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2. Using Every Trick in the Book: The Pla Surface Protease of Yersinia pestis

Author

Suomalainen, Marjo, Haiko, Johanna, Kukkonen, Maini, Korhonen, Timo K., Lähteenmäki, Kaarina, Virkola, Ritva, Westerlund-Wikström, Benita, Lobo, Leandro, Ramu, Päivi, Back, Nathan, Series Editor, Cohen, Irun R., Series Editor, Kritchevsky, David, Series Editor, Lajtha, Abel, Series Editor, Paoletti, Rodolfo, Series Editor, Perry, Robert D., editor, and Fetherston, Jacqueline D., editor

Published
2007
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3. Yersinia pestis Pla Has Multiple Virulence-associated Functions

Author

Lähteenmäki, Kaarina, Kukkonen, Maini, Jaatinen, Silja, Suomalainen, Marjo, Soranummi, Hanna, Virkola, Ritva, LÅng, Hannu, Korhonen, Timo K., Back, Nathan, editor, Cohen, Irun R., editor, Kritchevsky, David, editor, Lajtha, Abel, editor, Paoletti, Rodolfo, editor, Skurnik, Mikael, editor, Bengoechea, José Antonio, editor, and Granfors, Kaisa, editor

Published
2003
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4. Multifunctional Nature of Enterobacterial Fimbriae

Author

Korhonen, Timo K., Westerlund, Benita, Virkola, Ritva, Tarkkanen, Ann-Mari, Lähteenmäki, Kaarina, Kukkonen, Maini, Raunio, Tiina, Adegoke, Gabriel, Miettinen, Aaro, Clegg, Steven, Korhonen, Timo K., editor, Hovi, Tapani, editor, and Mäkelä, P. Helena, editor

Published
1992
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7. Functional Variability of Type 1 Fimbriae of Escherichia coli

Author

Pouttu, Riitta, Puustinen, Terhi, Kukkonen, Maini, Virkola, Ritva, Laurila, Minni, Hacker, Jörg, Klemm, Per, Korhonen, Timo K., Back, Nathan, editor, Cohen, Irun R., editor, Kritchevsky, David, editor, Lajtha, Abel, editor, Paoletti, Rodolfo, editor, Emoődy, Levente, editor, Pál, Tibor, editor, Hacker, Jörg, editor, and Blum-Oehler, Gabriele, editor

Published
2002
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11. The omptins of Yersinia pestis and Salmonella enterica cleave the reactive center loop of plasminogen activator inhibitor 1

Author

Haiko, Johanna, Laakkonen, Liisa, Juuti, Katri, Kalkkinen, Nisse, and Korhonen, Timo K.

Subjects
Yersinia pestis -- Physiological aspects, Antifibrinolytic agents -- Properties, Salmonella -- Physiological aspects, Cellular proteins -- Properties, Biological sciences
Abstract

Plasminogen activator inhibitor 1 (PAI-1) is a serine protease inhibitor (serpin) and a key molecule that regulates fibrinolysis by inactivating human plasminogen activators. Here we show that two important human pathogens, the plague bacterium Yersinia pestis and the enteropathogen Salmonella enterica serovar Typhimurium, inactivate PAI-1 by cleaving the R346-M347 bait peptide bond in the reactive center loop. No cleavage of PAI-1 was detected with Yersinia pseudotuberculosis, an oral/fecal pathogen from which Y. pestis has evolved, or with Escherichia coli. The cleavage and inactivation of PAI-1 were mediated by the outer membrane proteases plasminogen activator Pla of Y. pestis and PgtE protease of S. enterica, which belong to the omptin family of transmembrane endopeptidases identified in Gram-negative bacteria. Cleavage of PAI-1 was also detected with the omptins Epo of Erwinia pyrifoliae and Kop of Klebsiella pneumoniae, which both belong to the same omptin subfamily as Pla and PgtE, whereas no cleavage of PAI-1 was detected with omptins of Shigella flexneri or E. coli or the Yersinia chromosomal omptins, which belong to other omptin subfamilies. The results reveal a novel serpinolytic mechanism by which enterobacterial species expressing omptins of the Pla subfamily bypass normal control of host proteolysis. doi: 10.1128/JB.00458-10

Published
2010

12. Mat fimbriae promote biofilm formation by meningitis-associated Escherichia coli

Author

Lehti, Timo A., Bauchart, Philippe, Heikkinen, Johanna, Hacker, Jorg, Korhonen, Timo K., Dobrindt, Ulrich, and Westerlund-Wikstrom, Benita

Subjects
Meningitis -- Causes of, Meningitis -- Development and progression, Microbial mats -- Physiological aspects, Microbial mats -- Genetic aspects, Microbial mats -- Research, Escherichia coli -- Genetic aspects, Escherichia coli -- Research, Escherichia coli -- Physiological aspects, Biological sciences
Abstract

The mat (or ecp) fimbrial operon is ubiquitous and conserved in Escherichia coli, but its functions remain poorly described. In routine growth media newborn meningitis isolates of E. coil express the meningitis-associated and temperature-regulated (Mat) fimbria, also termed E. coli common pilus (ECP), at 20[degrees]C, and here we show that the six-gene (matABCDEF)-encoded Mat fimbria is needed for temperature-dependent biofilm formation on abiotic surfaces. The matBCDEF deletion mutant of meningitis E. coil IHE 3034 was defective in an early stage of biofilm development and consequently unable to establish a detectable biofilm, contrasting with IHE 3034 derivatives deleted for flagella, type 1 fimbriae or S-fimbriae, which retained the wild-type biofilm phenotype. Furthermore, induced production of Mat fimbriae from expression plasmids enabled biofilm-deficient E. coil K-1 2 cells to form biofilm at 20[degrees]C. No biofilm was detected with IHE 3034 or MG1655 strains grown at 37[degrees]C. The surface expression of Mat fimbriae and the frequency of Mat-positive cells in the IHE 3034 population from 20 [degrees]C were high and remained unaltered during the transition from planktonic to biofilm growth and within the matured biofilm community. Considering the prevalence of the highly conserved mat locus in E. coil genomes, we hypothesize that Mat fimbria-mediated biofilm formation is an ancestral characteristic of E. coil DOI 10.1099/mic.0.039610-0

Published
2010

13. The single substitution I259T, conserved in the plasminogen activator Pla of pandemic Yersinia pestis branches, enhances fibrinolytic activity

Author

Haiko, Johanna, Kukkonen, Maini, Ravantti, Janne J., Westerlund-Wikstrom, Benita, and Korhonen, Timo K.

Subjects
Thrombolytic drugs -- Research, Yersinia pestis -- Physiological aspects, Biological sciences
Abstract

The outer membrane plasminogen activator Pla of Yersinia pestis is a central virulence factor in plague. The primary structure of the Pla [beta]-barrel is conserved in Y. pestis biovars Antiqua, Medievalis, and Orientalis, which are associated with pandemics of plague. The Pla molecule of the ancestral Y. pestis lineages Microtus and Angola carries the single amino acid change T259I located in surface loop 5 of the [beta]-barrel. Recombinant Y. pestis KIM D34 or Escherichia coli XL1 expressing Pla T259I was impaired in fibrinolysis and in plasminogen activation. Lack of detectable generation of the catalytic light chain of plasmin and inactivation of plasmin enzymatic activity by the Pla T259I construct indicated that Microtus Pla cleaved the plasminogen molecule more unspecifically than did common Pla. The isoform pattern of the Pla T259I molecule was different from that of the common Pla molecule. Microtus Pla was more efficient than wild-type Pla in [[alpha].sub.2]-antiplasmin inactivation. Pla of Y. pestis and PgtE of Salmonella enterica have evolved from the same omptin ancestor, and their comparison showed that PgtE was poor in plasminogen activation but exhibited efficient antiprotease inactivation. The substitution [sup.259]IIDKT/TIDKN in PgtE, constructed to mimic the L5 region in Pla, altered proteolysis in favor of plasmin formation, whereas the reverse substitution [sup.259]TIDKN/IIDKT in Pla altered proteolysis in favor of [[alpha].sub.2]-antiplasmin inactivation. The results suggest that Microtus Pla represents an ancestral form of Pla that has evolved into a more efficient plasminogen activator in the pandemic Y. pestis lineages.

Published
2009

14. pH-dependent association of enolase and glyceraldehyde-3-phosphate dehydrogenase of Lactobacillus crispatus with the cell wall and lipoteichoic acids

Author

Antikainen, Jenni, Kupannen, Veera, Lahteenmaki, Kaarina, and Korhonen, Timo K.

Subjects
Enolase -- Research, Thrombolytic drugs -- Research, Binding proteins -- Research, Glyceraldehyde 3-phosphate dehydrogenase -- Research, Lactobacillus -- Genetic aspects, Lactobacillus -- Research, Biological sciences
Abstract

The plasminogen-binding proteins enolase and glyceraldehyde-3-phosphate dehydrogenase of Lactobacillus crispatus were localized on the cell surface at pH 5 but released into the medium at an alkaline pH. These proteins bound to lipoteichoic acids at a pH below their isoelectric point. The results indicate that lactobacilli rapidly modify their surface properties in response to changes in pH.

Published
2007

15. Extracellular proteins of Lactobacillus crispatus enhance activation of human plasminogen

Author

Hurmalainen, Veera, Edelman, Sanna, Antikainen, Jenni, Baumann, Marc, Lahteenmaki, Kaarina, and Korhonen, Timo K.

Subjects
Thrombolytic drugs -- Research, Lactobacillus -- Research, Bacterial proteins -- Research, Biological sciences
Abstract

The abundant proteolytic plasminogen (Plg)/plasmin system is important in several physiological functions in mammals and also engaged by a number of pathogenic microbial species to increase tissue invasiveness or to obtain nutrients. This paper reports that a commensal bacterium, Lactobacillus crispatus, interacts with the Pig system. Strain ST1 of L. crispatus enhanced activation of human Plg by the tissue-type Pig activator (tPA), whereas enhancement of the urokinase-mediated Plg activation was lower. ST1 cells bound Pig, plasmin and tPA only poorly, and the Plg-binding and activation-enhancing capacities were associated with extracellular material released from the bacteria into buffer. The extracellular proteome of L. crispatus ST1 contained enolase and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) as major components. The enolase and the GAPDH genes of ST1 were cloned, sequenced and expressed in recombinant Escherichia coli as [His.sub.6]-fusion proteins, which bound Plg and enhanced its activation by tPA. Variable levels of secretion of enolase and GAPDH proteins as well as of the Pig activation cofactor function were detected in strains representing major taxonomic groups of the genus Lactobacillus. So far, interference with the Plg system has been addressed with pathogenic microbes. The results reported here demonstrate a novel interaction between a member of the microbiota and a major proteolytic system in humans.

Published
2007

19. Evaluation of O-antigen inactivation on Pla activity and virulence of Yersinia pseudotuberculosis harbouring the pPla plasmid

Author

Pouillot, Flavie, Derbise, Anne, Kukkonen, Maini, Foulon, Jeannine, Korhonen, Timo K., and Carmel, Elisabeth

Subjects
Pseudotuberculosis -- Research, Yersinia infections -- Research, Plasmids -- Research, Biological sciences
Abstract

Yersinia pestis is a species that emerged recently from Yersinia pseudotuberculosis and gained an exceptional pathogenicity potential. Among the major genetic differences between the plague bacillus and its ancestor is the acquisition of the pPla plasmid, which has been associated with the increased virulence of Y. pestis. In a previous study, introduction of pPla into Y. pseudotuberculosis did not lead to any modification of the virulence of the host bacterium. However, it was subsequently demonstrated that the presence of smooth lipopolysaccharide (LPS) inhibits the activity of Pla. In this study, pPla was introduced into a Y. pseudotuberculosis strain expressing smooth LPS, and into a variant in which a mutation that abrogates the formation of O-antigen (O-Ag) repeats (as in natural isolates of Y. pestis) was generated. It was found that in both strains, Pla was synthesized, exported to the bacterial membrane and processed as in Y. pestis. However, the ability of Pla to activate plasminogen was weak and observed only at 37 [degrees]C in the smooth strain, while this activity was similar to that of Y. pestis and expressed at both 28 and 37 [degrees]C in the O-Ag mutant strain. Similarly, Pla-mediated inactivation of the antiprotease [[alpha].sub.2]-antiplasmin was not detected in the smooth Y. pseudotuberculosis strain grown at 28 [degrees]C, but was expressed at both temperatures in the O-Ag mutant strain. Despite the more efficient activity of Pla, the Y. pseudotuberculosis O-Ag mutant strain exhibited a lower pathogenicity upon subcutaneous infection of mice. The results thus indicate that, although abrogation of O side chain synthesis in a Y. pseudotuberculosis strain harbouring pPla potentiates the two proteolytic activities of Pla, this is not sufficient to confer to Y. pseudotuberculosis a higher pathogenicity potential. These results also suggest that acquisition of pPla may not have been sufficient to confer an immediate higher pathogenic potential to the ancestor Y. pestis strain.

Published
2005

20. The type III-dependent Hrp pilus is required for productive interaction of Xanthomonas campestris pv. vesicatoria with pepper host plants

Author

Weber, Ernst, Ojanen-Reuhs, Tuula, Huguet, Elisabeth, Hause, Gerd, Romantschuk, Martin, Korhonen, Timo K., Bonas, Ulla, and Koebnik, Ralf

Subjects
Bacteriology -- Research, Bacteria, Pathogenic -- Research, Biological sciences
Abstract

The plant pathogenic bacterium Xanthomonas campestris pv. vesicatoria expresses a type III secretion system that is necessary for both pathogenicity in susceptible hosts and the induction of the hypersensitive response in resistant plants. This specialized protein transport system is encoded by a 23-kb hrp (hypersensitive response and pathogenicity) gene cluster. Here we show that X. campestris pv. vesicatoria produces filamentous structures, the Hrp pili, at the cell surface under hrp-inducing conditions. Analysis of purified Hrp pili and immunoelectron microscopy revealed that the major component of the Hrp pilus is the HrpE protein which is encoded in the hrp gene cluster. Sequence homologues of hrpE are only found in other xanthomonads. However, hrpE is syntenic to the hrpY gene from another plant pathogen, Ralstonia solanacearum. Bioinformatic analyses suggest that all major Hrp pilus subunits from gram-negative plant pathogens may share the same structural organization, i.e., a predominant alpha-helical structure. Analysis of nonpolar mutants in hrpE demonstrated that the Hrp pilus is essential for the productive interaction of X. campestris pv. vesicatoria with pepper host plants. Furthermore, a functional Hrp pilus is required for type III-dependent protein secretion. Immunoelectron microscopy revealed that type III-secreted proteins, such as HrpF and AvrBs3, are in close contact with the Hrp pilus during and/or after their secretion. By systematic analysis of nonpolar hrp/hrc (hrp conserved) and hpa (hrp associated) mutants, we found that Hpa proteins as well as the translocon protein HrpF are dispensable for pilus assembly, while all other Hrp and Hrc proteins are required. Hence, there are no other conserved Hrp or Hrc proteins that act downstream of HrpE during type III-dependent protein translocation.

Published
2005

23. In vitro adhesion specificity of indigenous Lactobacilli within the avian intestinal tract

Author

Edelman, Sanna, Westerlund-Wikstrom, Benita, Leskela, Susanna, Kettunen, Hannele, Rautonen, Nina, Apajalahti, Juha, and Korhonen, Timo K.

Subjects
Lactobacillus -- Physiological aspects, Host-bacteria relationships -- Physiological aspects, Birds, Bacteria -- Adhesion, Biological sciences
Abstract

Cell adhesion analysis shows that fresh lactobacillus cells adhere to the epithelium and in a strain-dependent manner, the cells adhere to follicle-associated epithelium and the apical surfaces of mature endocytes of intestinal villi.

Published
2002

24. Identification by flagellum display of an epithelial cell- and fibronectin-binding function in the SlpA surface protein of Lactobacillus brevis

Author

Hynonen, Ulla, Westerlund-Wikstrom, Benita, Palva, Airi, and Korhonen, Timo K.

Subjects
Bacteria -- Adhesion, Flagella (Microbiology) -- Physiological aspects, Cell receptors -- Physiological aspects, Protein binding -- Physiological aspects, Biological sciences
Abstract

Research demonstrates that the S-layer of the SlpA surface protein mediattes Lactobacillus brevis ATCC 8287 adhesion to human epithelial cells and fibronectin. The receptor-binding region is confined to a region of 81 amino acids in the N-terminal part of the S-layer.

Published
2002

25. matB, a common fimbrillin gene of Escherichia coli, expressed in a genetically conserved, virulent clonal group

Author

Pouttu, Riitta, Westerlund-Wikstrom, Benita, Lang, Hannu, Alsti, Krista, Virkola, Ritva, Saarela, Ulla, Siitonen, Anja, kalkkinen, Nisse, and Korhonen, Timo K.

Subjects
Escherichia coli -- Genetic aspects, Bacteria -- Adhesion, Gene expression -- Analysis, Genetic transcription -- Analysis, Biological sciences
Abstract

Results show that the matB fimbrial gene is expressed only in a geneticlly conserved, virulent Escherichica coli strain. Data suggest that regulation of Mat fimbria expression involves transcriptional and posttranslational events.

Published
2001

26. The gaf fimbrial gene cluster of Escherichia coli expresses a full-size and a truncated soluble adhesin protein

Author

Tanskanen, Jarna, Saarela, Sirkku, Tankka, Sanna, Kalkkinen, Nisse, Rhen, Mikael, Korhonen, Timo K., and Westerlund-Wikstrom, Benita

Subjects
Escherichia coli -- Genetic aspects, Cell adhesion molecules -- Genetic aspects, Protein binding -- Analysis, Binding sites (Biochemistry) -- Analysis, Structure-activity relationships (Biochemistry) -- Analysis, Biological sciences
Abstract

Research describes construction and purification of gaf gene cluster encoded GafD lectin from Escherichia coli for structure-function analysis of the fimbrial adhesisn protein. Results show that GafD is a soluble non-fusion form of the lectin and its protease-resistant subdomain exhibits receptor-binding specificity.

Published
2001

27. Expression of cbsA encoding the collagen-binding S-protein of Lactobacillus crispatus JCM5810 in Lactobacillus casei ATCC 393 (super)T

Author

Martinez, Beatriz, Sillanpaa, Jouko, Smit, Egbert, Korhonen, Timo K., and Pouwels, Peter H.

Subjects
Bacteriology -- Research, Lactobacillus -- Genetic aspects, Gene expression -- Physiological aspects, Carrier proteins -- Research, Collagen -- Physiological aspects, Biological sciences
Abstract

Research has been conducted on the collagen-binding S-layer protein of Lactobacillus crispatus JCM5810. The cbsA gene encoding of this protein has been expressed in Lactobacillus casei ATCC 393 (super)T and the results indicate that S-protein was secreted into the medium of the recombinant bacteria.

Published
2000

28. Characterization of the collagen-binding S-layer protein CbsA of Lactobacillus crispatus

Author

Sillanpaa, Jouko, Martinez, Beatriz, Antikainen, Jenni, Toba, Takahiro, Kalkkinen, Nisse, Tankka, Sanna, Lounatmaa, Kari, Keranen, Jaakko, Hook, Magnus, Westerlund-Wikstrom, Benita, Pouwels, Peter H., and Korhonen, Timo K.

Subjects
Protein binding -- Analysis, Lactobacillus -- Physiological aspects, Collagen -- Physiological aspects, Cell adhesion -- Molecular aspects, Biological sciences
Abstract

Results show that the collagen-binding S-layer protein CbsA is a polypeptide of 410 amino acids with a stronger collagen-binding region at the N-terminus and a weaker one at the C-terminus. Data further indicate that collagen-binding requires a crystal structure with regular array of CbsA.

Published
2000

29. Construction of a multihybrid display system: flagellar filaments carrying two foreign adhesive peptides

Author

Tanskanen, Jarna, Korhonen, Timo K., and Westerlund-Wikstrom, Benita

Subjects
Flagella (Microbiology) -- Physiological aspects, Recombinant molecules -- Usage, Peptides -- Analysis, Escherichia coli -- Research, Biological sciences
Abstract

Research describes construction of a flagellum carrying two different recombinant flagellins of flagellin subunits in Escherichia coli. Data demonstrate that a fibronectin-binding 115-mer peptide and a 302-mer collagen-binding peptide can be inserted into a flagellum as revealed by adhesion and immunochemical tests.

Published
2000

34. Contributors

Author

Adachi, Hideki, primary, Adachi, Osao, additional, Adam, Zach, additional, Adams, Michael W.W., additional, Adang, Michael J., additional, Adham, Ibrahim M., additional, Aducci, Patrizia, additional, Agard, David A., additional, Agranovsky, Alexey A., additional, Ahn, Kyunghye, additional, Akiyama, Yoshinori, additional, Alejo, Alí, additional, Amberg, Sean M., additional, Amerik, Alexander Y., additional, Andrés, Germán, additional, Andrews, Robert K., additional, Antalis, Toni M., additional, Apte, Suneel S., additional, Arima, Kazunari, additional, Arlaud, Gérard J., additional, Aronson, Nathan N., additional, Asano, Yasuhisa, additional, Ascenzi, Paolo, additional, Assakura, Marina T., additional, Auld, David S., additional, Avilés, Francesc X., additional, Awad, William M., additional, Babé, Lilia M., additional, Badorff, Cornel, additional, Bai, Shan, additional, Baird, Teaster T., additional, Paul Bajaj, S., additional, Baker, Rohan T., additional, Baker, Susan C., additional, Ballinger, Marcus D., additional, Banbula, Agnieszka, additional, Bannikov, Gregory A., additional, Barrett, Alan J., additional, Bartlett, John D., additional, Baskova, Isolda P., additional, Bauer, Karl, additional, Baumann, Ulrich, additional, Baumeister, Wolfgang, additional, Beauvais, Anne, additional, Belas, Robert, additional, Beppu, Teruhiko, additional, Bergmann, Ernst M., additional, Bergo, Martin O., additional, Berndt, Michael C., additional, Berry, Colin, additional, Bertenshaw, Greg P., additional, Betzel, Ch., additional, Bierbaum, Gabriele, additional, Bieth, Joseph G., additional, Bjarnason, Jón B., additional, Blaber, M., additional, Blaber, S.I., additional, Black, Roy A., additional, Blackman, M.J., additional, Blinkovsky, Alexander, additional, Blobel, Carl P., additional, Boatright, Kelly M., additional, Böck, August, additional, Boeke, Jef D., additional, Boileau, Guy, additional, Bolken, Tové C., additional, Bond, Judith S., additional, Bordallo, Javier, additional, Bordusa, Frank, additional, Boucaut, Kerry J., additional, Bouvier, Jacques, additional, Bowman, Barry J., additional, Bradshaw, Ralph A., additional, Braun, Hans-Peter, additional, Breddam, Klaus, additional, Brindley, Paul J., additional, Broadhurst, Anne, additional, Brocklehurst, Keith, additional, Broder, Dan H., additional, Brömme, Dieter, additional, Bron, Sierd, additional, Broom, Murray, additional, Brown, Kenneth D., additional, Brown, Mark A., additional, Bunn, Rhonda, additional, Burleigh, Barbara A., additional, Butler, Michael J., additional, Buttle, David J., additional, Byrd, Chelsea M., additional, Byun, Tony, additional, Cadel, Sandrine, additional, Caffrey, Conor R., additional, Caldentey, Javier, additional, Caprioglio, Daniel R., additional, Carbonell, Juan, additional, Carpentier, Mélanie, additional, Carter, Ruth E., additional, Casey, Patrick J., additional, Castellino, Francis J., additional, Catanese, Joseph J., additional, Caterson, Bruce, additional, Caughey, George H., additional, Cawley, Niamh X., additional, Cawston, Tim E., additional, Jose Cazzulo, Juan, additional, Cercós, Manuel, additional, Chakraborty, Trinad, additional, Chambers, Henry F., additional, Chang, L.S., additional, Chan, Michael K., additional, Chan, Sunney I., additional, Chao, Julie, additional, Chapot-Chartier, Marie-Pierre, additional, Chave, Karen J., additional, Chen, Jian-Min, additional, Chen, Jinq-May, additional, Chesneau, Valérie, additional, Chevrier, Bernard, additional, Chich, Jean-François, additional, Yong Choi, Kwan, additional, Chrétien, Michel, additional, Ha Chung, Chin, additional, Chung, Dominic W., additional, Clamagirand, Christine, additional, Clark, Ian M., additional, Clarke, Adrian K., additional, Clarke, Steven, additional, Cleary, Paul P., additional, Clements, Judith A., additional, Cleuziat, Philippe, additional, Cohen, Paul, additional, Colige, Alain, additional, Collen, D., additional, Collier, Ivan E., additional, Colloms, Sean D., additional, Colman, Robert W., additional, Conner, Gregory E., additional, Conzelmann, Andreas, additional, Coolbear, Tim, additional, Coombs, Graham H., additional, Cooper, Jonathan B., additional, Cooper, Max D., additional, Copeland, Nikki A., additional, Corvol, Pierre, additional, Cottrell, Graeme S., additional, Coyle, Joseph T., additional, Craik, Charles S., additional, Creemers, John W.M., additional, Croce, Jenifer, additional, Cueva, Rosario, additional, Cutting, Simon, additional, d′Enfert, Christophe, additional, D′Orchymont, Hugues, additional, Daenke, S., additional, Dahlbäck, Björn, additional, Dalbey, Ross E., additional, Dalton, John P., additional, Dando (Deceased), Pamela M., additional, Daniel, R.M., additional, Darke, Paul L., additional, Lagerblad de Oliveira, Pedro, additional, de Vos, Sarah, additional, Deghmane, Ala-Eddine, additional, Dekker, Niek, additional, DeLotto, Robert, additional, DeMartino, George N., additional, den Boon, Johan A., additional, Denison, Mark R., additional, DesGroseillers, Luc, additional, Deussing, Jan, additional, Devi, Lakshmi A., additional, Diamandis, Eleftherios P., additional, Dickson, Robert B., additional, Dingwall, Colin, additional, Dixon, Jack E., additional, Dodt, Johannes, additional, Dolenc, Iztoc, additional, Cat Dong, Tran, additional, Dong, Ying, additional, Dubois, Jean-Yves F., additional, Dudley, Edward G., additional, Dunn, Ben M., additional, Dupuy, Bruno, additional, Conceicão Duque-Magalhães, Maria, additional, Eeckhout, Yves, additional, Egelrud, Torbjörn, additional, Eijsink, Vincent, additional, Ellis, Vincent, additional, Engel, Wolfgang, additional, Erdös, Ervin G., additional, Etscheid, Michael, additional, Evans (Deceased), Herbert J., additional, Everett, Roger D., additional, Eyries, Mélanie, additional, Fahrenholz, Falk, additional, Fenster, Kurt M., additional, Férec, Claude, additional, Henrique Ferreira Sorgine, Marcos, additional, Fink, Doran, additional, Fives-Taylor, Paula M., additional, Foltmann, Bent, additional, Foster, Simon J., additional, Foulon, Thierry, additional, Foundling, Stephen I., additional, Fox, Jay W., additional, Freeze, Hudson H., additional, Frère, Jean-Marie, additional, Frey, Teryl K., additional, Flicker, Lloyd D., additional, Fritsche, Erich, additional, Froelich, Christopher J., additional, Fuhrmann, Cynthia N., additional, Fujimura, Satoshi, additional, Fukushima, J., additional, Fuller, Robert S., additional, Gaboriaud, Christine, additional, Gache, Christian, additional, Galivan, John, additional, Gary, Jonathan D., additional, Gaucher, G.M., additional, Ghuysen, Jean-Marie, additional, Gil, María J., additional, Giller, Thomas, additional, Goffin, Colette, additional, Gohda, Eiichi, additional, Goldberg, Alfred L., additional, Goldberg, Daniel E., additional, Goldberg, Gregory I., additional, Gorbalenya, Alexander E., additional, Gordon, Stuart G., additional, Götz, Friedrich, additional, Gráf, László, additional, Granados, Robert R., additional, Granell, Antonio, additional, Graycar, Thomas P., additional, Green, Jonathan, additional, Greenspan, Daniel S., additional, Grubman, Marvin J., additional, Grunden, Amy M., additional, Guillemain, Bernard, additional, Guinand, Micheline, additional, Gutiérrez, José Maria, additional, Haeggström, Jesper Z., additional, Hageman, James H., additional, Hagmann, Marie-Luise, additional, Halfon, Sherin, additional, Hamilton, Andrew J., additional, Seon Han, Ji, additional, Hara-Nishimura, Ikuko, additional, Harada, Minoru, additional, Hartzell, William O., additional, Hay, Rod J., additional, Hayashi, Kiyoshi, additional, Hendriks, Dirk F., additional, Henrich, Bernhard, additional, Henriet, Patrick, additional, Hernández-Arana, Andrés, additional, Herrera-Camacho, Irma, additional, Heusipp, Gerhard, additional, Hicks, P.M., additional, Hillman, Bradley I., additional, Yukihiro Hiraoka, B., additional, Hiratake, Jun, additional, Ho, Heng-Chien, additional, Thi Hoa, Ngo, additional, Hochstrasser, Mark, additional, Hofmann, Theo, additional, Hohn, Thomas, additional, Hoidal, John R., additional, Holbrook, Joanna D., additional, Höltje, Joachim-Volker, additional, Homma, Koichi J., additional, Hook, Vivian Y.H., additional, Hooper, John D., additional, Hooper, Nigel M., additional, Hosoi, Kazuo, additional, Hospital, Véronique, additional, Howe, Christopher J., additional, Hruby, Dennis E., additional, Huang, H.-C., additional, Huber, Robert, additional, Hughes, Clare E., additional, Ibrahim-Granet, Oumaïma, additional, Ichishima, Eiji, additional, Ikehara, Yukio, additional, Imamura, Takahisa, additional, Inagaki, Noritoshi, additional, Inagami, Tadashi, additional, Isaac, R.E., additional, Isaya, Grazia, additional, Ishihara, Kohji, additional, Ishii, Shin-ichi, additional, Itoh, Yoshifumi, additional, Ito, Kiyoshi, additional, Ito, Koreaki, additional, Iwanaga, Sadaaki, additional, Jack, Ralph W., additional, Jackson, Mel C., additional, James, Michael N.G., additional, Jeffrey (Deceased), John, additional, Jiang, Ping, additional, Johnson, Gary D., additional, Johnson, John E., additional, Johnson, Michael, additional, Albert Johnston, Stephen, additional, Jones, Elizabeth W., additional, Jongbloed, Jan D.H., additional, Joshua-Tor, Leemor, additional, Joudiou, Carine, additional, Juliano, Luiz, additional, Jupp, Ray, additional, Kaminogawa, Shuichi, additional, Kamio, Yoshiyuki, additional, Kan, Chen-Chen, additional, Kaneda, Makoto, additional, Gyun Kang, Sung, additional, Kania, Mary, additional, Kanjanahaluethai, Amornrat, additional, Kawabata, Shun-ichiro, additional, Kay, John, additional, Keiler, Kenneth C., additional, Kelly, R.M., additional, Kerr, Michael A, additional, Kervinen, Jukka, additional, Kessler, Efrat, additional, Kidd, Simon, additional, Kilian, Mogens, additional, Kim, Do-Hyung, additional, Seop Kim, In, additional, Kimura, Yukio, additional, Kirisako, Takayoshi, additional, Kirschke, Heidrun, additional, Kishi, Tadaaki, additional, Kitamura, Naomi, additional, Kitazono, Ana A., additional, Kleanthous, Colin, additional, Klein, Jürgen R., additional, Kobayashi, Hideyuki, additional, Koelsch, Gerald, additional, Kok, Jan, additional, Kolattukudy, P.E., additional, Kolmar, Harald, additional, Komori, Yumiko, additional, Konvalinka, Jan, additional, Korhonen, Timo K., additional, Kortt, Alexander A., additional, Kräusslich, Hans-Georg, additional, Kress, Lawrence F., additional, Kubo, Takeaki, additional, Kukkonen, Maini, additional, Kumagai, Hidehiko, additional, Kumazaki, Takashi, additional, Kümmerer, Beate M., additional, Kuno, Kouji, additional, Kurachi, Kotoku, additional, Kurkinen, Markku, additional, Lähteenmäki, Kaarina, additional, Laing, Gavin D., additional, Lambkin, Imelda J., additional, Lamppa, Gayle K., additional, Lång, Hannu, additional, Langer, Thomas, additional, Laursen, Richard A., additional, Le Bonniec, Bernard F., additional, Luel Lee, Bok, additional, Joon Lee, Kye, additional, Young Lee, So, additional, Lee, Soohee, additional, Leis, Jonathan, additional, LeMosy, Ellen K., additional, Lepage, Thierry, additional, Leppla, Stephen H., additional, Lessard, Ivan A.D., additional, Lhomond, Guy, additional, Liao, Ta-Hsiu, additional, Lieber, Toby, additional, Lijnen, H.R., additional, Lima, Christopher D., additional, Lin, Chen-Yong, additional, Lin, Xinli, additional, Lindsay, L.L., additional, Lipscomb, William N., additional, Little, Christopher B., additional, Little, John W., additional, Lively, Mark O., additional, Lobel, Peter, additional, Peng Loh, Y., additional, Lohi, Jouko, additional, Lomonossoff, G.P., additional, Looze, Yvan, additional, López-García, Alma, additional, López-Otín, Carlos, additional, Luo, Liu-Ying, additional, Lupas, Andrei, additional, MacKay, Vivian L., additional, Mains, Richard E., additional, Mäkinen, Kauko K., additional, Mäkinen, Pirkko-Liisa, additional, Mandelbaum, Fajga R., additional, Manning, James M., additional, Marcotrigiano, Joseph, additional, Markland, Francis S., additional, Maruyama, M., additional, Maruyama, Sususmu, additional, Masaki, Takeharu, additional, Mathew, Zacharia, additional, Matrisian, Lynn M., additional, Matsuda, Yoshihiro, additional, Matsuka, Yury V., additional, Matsushita, Osamu, additional, Matsuzawa, Hiroshi, additional, Maurizi, Michael R., additional, Mbikay, Majambu, additional, Ken McDonald, J., additional, McKerrow, James H., additional, McMillan, David, additional, Mecham, Robert P., additional, Mehta, Darshini P., additional, Meighan, Paul, additional, Mellors, Alan, additional, Melton, Roger G., additional, Ménard, Armelle, additional, Ménard, Robert, additional, Menéndez-Arias, Luis, additional, Meyer, Diane H., additional, Meyers, Gregor, additional, Michaelis, Susan, additional, Mielicki, Wojciech P., additional, Mierau, Igor, additional, Millán-Pérez-Peña, Lourdes, additional, Miller, Charles G., additional, Mills, John, additional, Mills, Kenneth V., additional, Mistou, Michel-Yves, additional, Misumi, Yoshio, additional, Miyoshi, Shin-ichi, additional, Mizutani, Shigehiko, additional, Mock, William L., additional, Möhrlen, Frank, additional, Moiré, Nathalie, additional, Monnet, Véronique, additional, Monod, Michel, additional, Montecucco, Cesare, additional, Morita, Takashi, additional, Morrissey, James H., additional, Mort, John S., additional, Mortensen, Uffe H., additional, Morty, Rory E., additional, Motoshima, Hidemasa, additional, Mottram, Jeremy C., additional, Mundt, Egbert, additional, Murakami, Kazuo, additional, Murakami-Murofushi, Kimiko, additional, Murao, Sawao, additional, Murata, Christina, additional, Murphy, Gillian, additional, Muta, Tatsushi, additional, Mzhavia, Nino, additional, Nagase, Hideaki, additional, Naik, Rajesh R., additional, Nakajima, Nobuyoshi, additional, Nakamura, Hiroyuki, additional, Nakamura, Yukio, additional, Nasmyth, Kim, additional, Navarro-García, Fernando, additional, Netzel-Arnett, Sarah, additional, Nguyen-Distéche, Martine, additional, Nicholson, Donald, additional, Nikai, Toshiaki, additional, Nirasawa, Satoru, additional, Nishii, Wataru, additional, Nishiyama, Makoto, additional, Niven, Gordon W., additional, Nomura, Seiji, additional, Norioka, Shigemi, additional, North, Michael J., additional, Nuss, Donald L., additional, O′Connor, Michael B., additional, Oberst, Michael, additional, Oda, Kohei, additional, Odorico, Dimitri M., additional, Oetjen, Joyce, additional, Ogura, Teru, additional, Ohkubo, Iwao, additional, Ohlendorf, Douglas H., additional, Ohman, Dennis E., additional, Ohsumi, Yoshinori, additional, Okabe, Akinobu, additional, Okuda, K., additional, Olesen, Kjeld, additional, Oroszlan, Stephen, additional, Orth, Kim, additional, Ota, Nobuyuki, additional, Ovadia, Michael, additional, Overgaard, Michael T., additional, O-Wang, Jiyang, additional, Oxvig, Claus, additional, Packer, Jeremy C.L., additional, Paetzel, Mark, additional, Paine, Mark J.I., additional, Park, John E., additional, Woo Park, Pyong, additional, Soo Park, Sung, additional, Parkin, Kirk L., additional, Parks, William C., additional, Pascall, John C., additional, Paschos, Athanasios, additional, Paul, Sudhir, additional, Pearce, David A., additional, Pei, Duanqing, additional, Pemberton, Alan D., additional, Peters, Jan-Michael, additional, Phylip, Lowri H., additional, Pichová, Iva, additional, Pieper, Michael, additional, Piesse, Christophe, additional, Pike, Rob, additional, Pinck, Lothaire, additional, Pirzad, Ramin, additional, Pitot, Henry C., additional, Plaut, Andrew G., additional, Polgár, László, additional, Postina, Rolf, additional, Potempa, Jan, additional, Poulsen, Knud, additional, Pritchard, David G., additional, Pshezhetsky, Alexey V., additional, Abul Qasim, M., additional, Rader, Stephen D., additional, Rando, Robert R., additional, Rao, Mala, additional, Rao, Narayanam V., additional, Ratnoff, Oscar D., additional, Rawlings, Neil D., additional, Rawson, Robert B., additional, Reddy, Vijay, additional, Redman, Colvin M., additional, Reichl (Deceased), Antonia P., additional, Reid, Julian R., additional, Reid, Kenneth B.M., additional, Remaut, Han, additional, James Remington, S., additional, Rettig, Wolfgang J., additional, Rholam, Mohamed, additional, Rice, Charles M., additional, Richter, Stefan, additional, Riezman, Howard, additional, Ritchie, Alison, additional, Ro, Hyo-Sung, additional, Robert-Baudouy, Janine, additional, Michael Roberts, R., additional, Robinson, Michael, additional, Rodríguez-Romero, Adela, additional, Rogers, John C., additional, Rosenthal, Philip J., additional, Rose, A.M., additional, Rosing, J., additional, Rossetto, Ornella, additional, Rossi, Cesare, additional, Rossi, Véronique, additional, Roth, Richard A., additional, Rowan, Andrew D., additional, Rozanov, Mikhail, additional, Rucavado, Alexandra, additional, Rul, Françoise, additional, Rümenapf, Tillmann, additional, Ryan, Martin D., additional, Ryan, Thomas J., additional, Sacco, Elena, additional, Evan Sadler, J., additional, Saenger, W., additional, Sahl, Hans-Georg, additional, Sajid, Mohammed, additional, Sakiyama, Fumio, additional, Salas, María L., additional, Salter, Jason P., additional, Salvesen, Guy S., additional, Sanchez, Eladio F., additional, Sang, Qing-Xiang Amy, additional, Sankaran, Krishnan, additional, Sarras, Michael P., additional, Sasagawa, Yoshikiyo, additional, Satoh, Kimiyuki, additional, Sauer, Robert T., additional, Sawada, Hitoshi, additional, Scarisbrick, I.A., additional, Schauer-Vukasinovic, Vesna, additional, Schlievert, Patrick M., additional, Schlösser, Manfred, additional, Schmidt, Amy E., additional, Schmidt, Brian F., additional, Schmidt, Walter K., additional, Schmitz, Udo K., additional, Schneemann, Anette, additional, Scholze, Henning, additional, Schomburg, Lutz, additional, Schwaeble, Wilhelm J., additional, Sedlacek, Radislav, additional, Seemüller, Erika, additional, Seidah, Nabil G., additional, Seiki, Motoharu, additional, Selistre de Araujo, Heloisa S., additional, Senior, Robert M., additional, Sik Seong, Ihn, additional, Serpe, Mihaela, additional, Serrano, Solange M.T., additional, Setlow, Peter, additional, Shanks, M., additional, Shao, Feng, additional, Shapiro, Steven D., additional, Shen, Lei, additional, Sherwood (Deceased), Roger F., additional, Shi, Yun-Bo, additional, Shimoi, Hitoshi, additional, Shinoda, Sumio, additional, Siigur, Ene, additional, Siigur, Jüri, additional, Sim, Robert B., additional, Simmer, James P., additional, Simmons, William H., additional, Sirakova, Tatiana D., additional, Skern, Tim, additional, Skidgel, Randal A., additional, Slack, Jeffrey, additional, Sleat, David E., additional, Smith, Janet L., additional, Smyth, Mark J., additional, Snijder, Eric J., additional, Söderhäll, Kenneth, additional, Sohar, Istvan, additional, Sorimachi, Hiroyuki, additional, Sottrup-Jensen, Lars, additional, Soubrier, Florent, additional, Soukhodolets, Karen E., additional, Springman, Eric B., additional, Geme, Joseph W. St., additional, Leger, Raymond J. St., additional, Steele, James L., additional, Steinkühler, Christian, additional, Stenberg, Leisa M., additional, Stenflo, Johan, additional, Stennicke, Henning R., additional, Stepanov (Deceased), Valentin M., additional, Steven, Frank, additional, Stevenson, Kenneth J., additional, Stewart, David J., additional, Storer, Andrew C., additional, Stover, Cordula, additional, Sträter, Norbert, additional, Strauss, Ellen G., additional, Strauss, James H., additional, Stöcker, Walter, additional, Stříšovský, Kvido, additional, Suárez-Rendueles, Paz, additional, Sugimoto, Manabu, additional, Sulea, Traian, additional, Suzuki, Fumiaki, additional, Suzuki, Hideyuki, additional, Swenson, Stephen, additional, Szecsi, Pal B., additional, Szilágyi, László, additional, Taha, Muhamed-Kheir, additional, Takahashi, Kenji, additional, Takio, Koji, additional, Tamura, Tomohiro, additional, Tan, Fulong, additional, Hong Tan, Nget, additional, Tanase, Carmen, additional, Tang, Jordan, additional, Tanizaki, Martha M., additional, Tannich, Egbert, additional, Tans, G., additional, Tarentino (Deceased), Anthony L., additional, Tatnell, Peter J., additional, Tatsumi, Hiroki, additional, Tautz, Norbert, additional, Templin, Markus F., additional, Terada, Shigeyuki, additional, Thacker, C., additional, Theodoratou, Ekaterini, additional, Thiel, Heinz-Jürgen, additional, Thielens, Nicole M., additional, Thierry, Gonzales, additional, Thomas, Mark D., additional, Thornberry, Nancy A., additional, Thorsness, Mary K., additional, Thorsness, Peter E., additional, Tigue, Natalie J., additional, Tjalsma, Harold, additional, Tomkinson, Birgitta, additional, Tonello, Fiorella, additional, Toogood, H.S., additional, Toombs, Christopher, additional, Tortora, Paolo, additional, Tözsér, József, additional, Travis, James, additional, Tschesche, Harald, additional, Tsujimoto, Masafumi, additional, Tsunasawa, Susumu, additional, Tsu, Christopher A., additional, Tu, Anthony T., additional, Turk, Boris, additional, Turk, Dusan, additional, Turk, Vito, additional, Turner, Anthony J., additional, Uchikoba, Tetsuya, additional, Uitto, Veli-Jukka, additional, Ullmann, Dirk, additional, Valdenaire, Olivier, additional, Van Beeumen, Jozef, additional, Van de Ven, Wim J.M., additional, van den Burg, Bertus, additional, Maarten van Dijl, Jan, additional, van Roosmalen, Maarten L., additional, Van Wart, Harold E., additional, Vanoni, Marco, additional, Vath, Gregory M., additional, Velasco, Gloria, additional, Vendrell, Josep, additional, Venekei, István, additional, Vera, Pablo, additional, Verchot-Lubicz, Jeanmarie, additional, Vines, Richard R., additional, Volanakis, John E., additional, Wagner, Fred W., additional, Wainwright, Shane W., additional, Walker, Kenneth W., additional, Walker, Stephen J., additional, Wallach, Jean, additional, Walling, Linda L., additional, Walsh, Peter N., additional, Wang, P., additional, May Wang, Q., additional, Wassenaar, Alfred L.M., additional, Watts, Aaron B., additional, Weber, Joseph M., additional, Webster, Daniel R., additional, Weiss, Stephen J., additional, Wells, James A., additional, Wenzel, Herbert, additional, Wewer, Ulla M., additional, White, Judith M., additional, Wilk, Sherwin, additional, Wilkin, Jean-Marc, additional, Wilkins, Tracy D., additional, Wilkinson, Keith D., additional, Winther, Jakob R., additional, Wlodawer, Alexander, additional, Fred Woessner, J., additional, Wolfe, Michael S., additional, Wolfsberg, Tyra G., additional, Woodgate, Roger, additional, Wright, G.D., additional, Wu, Qingyu, additional, Xie, Sancai, additional, Yamagami, Kenjiro, additional, Yamaguchi, Nozomi, additional, Yamakawa, Yoshio, additional, Yamamoto, Kei, additional, Yamamoto, Shigeo, additional, Yana, Ikuo, additional, Yang, Maozhou, additional, Yasuda, Noriko, additional, Yasuhara, Toshimasa, additional, Yasumasu, Shigeki, additional, Yi, Elizabeth, additional, Yiallouros, Irene, additional, Yonezawa, Hiroo, additional, Ji Yoo, Soon, additional, Yoshimoto, Tadashi, additional, Young, Michael W., additional, Young, Stephen G., additional, Zavalova, Ludmila L., additional, Zdanov, Alexander, additional, and Zhang, Hong-Zhong, additional

Published
2004
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35. Characterization of the fimA gene encoding bundle-forming fimbriae of the plant pathogen Xanthomonas campestris pv. vesicatoria

Author

Ojanen-Reuhs, Tuula, Kalkkinen, Nisse, Westerlund-Wikstrom, Benita, Doorn, Joop van, Haahtela, Kielo, Nurmiaho-Lassila, Eeva-Liisa, Wengelnik, Kai, Bonas, Ulla, and Korhonen, Timo K.

Subjects
Bacteria, Phytopathogenic -- Genetic aspects, Virulence (Microbiology) -- Genetic aspects, Biological sciences
Abstract

The Xanthomonas capestris fimA gene encoding the bundle-forming fimbriae and cell aggregation was analyzed to characterize the role of fimbriae in Xanthomonas capestris infections. The nucleotide sequence of the fimA gene of Xanthomonas campestris was composed of two open reading frames that encode FimA and FimB proteins. Mutations in the fimA gene also impaired cell aggregation and reduced the virulence of Xanthomonas campestris cells in infected tomato leaves.

Published
1997

38. A collagen-binding S-layer in Lactobacillus crispatus

Author

Toba, Takahiro, Virkola, Ritva, Westerlund, Benita, Bjorkman, Yvonne, Sillanpaa, Jouko, Vartio, Tapio, Kalkkinen, Nisse, and Korhonen, Timo K.

Subjects
Lactobacillus -- Research, Biological sciences
Abstract

Lactobacillus acidophilus commonly inhabits the intestinal tract of both man and animal. The S-layer of Lactobacillus crispatus JCM 5810 of A2 strain acts as specific bacterial adhesin and initiates bacterial adhesion to the mammalian extracellular matrix (ECM), thereby providing direct evidence that normal intestinal bacterial flora can adhere to the subintestinal ECM. S layers commonly occur in lactic acid bacteria. JCM 5810 of the S-layer has high affinity towards I and IV collagen and exhibits functional heterogeneity.

Published
1995

40. Outer membrane proteins and lipopolysaccharides in pathovars of Xanthomonas campestris

Author

Ojanen, Tuula, Helander, Ilkka M., Haahtela, Kielo, Korhonen, Timo K., and Laakso, Tuula

Subjects
Endotoxins -- Research, Membrane proteins -- Analysis, Gel electrophoresis -- Usage, Biological sciences
Abstract

An analysis of the outer membrane protein (OMP) and lipopolysaccharide (LPS) patterns of 54 isolates of 16 distinct pathovars of Xanthomonas campestris reveals that the strains within a single pathovar are almost identical to isolates from other pathovars. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) aids the analysis of the characteristic features of OMPs and LPSs of X. campestris. Within X. campestris pv. translucens, X. campestris pv. campestris and X campestris pv. vesicatoria, profiles of LPSs and OMPs differ from each other.

Published
1993

43. Molecular adaptation of a plant-bacterium outer membrane protease towards plague virulence factor Pla

Author

Westerlund-Wikström Benita, Laakkonen Liisa, Haiko Johanna, and Korhonen Timo K

Subjects
Evolution, QH359-425
Abstract

Abstract Background Omptins are a family of outer membrane proteases that have spread by horizontal gene transfer in Gram-negative bacteria that infect vertebrates or plants. Despite structural similarity, the molecular functions of omptins differ in a manner that reflects the life style of their host bacteria. To simulate the molecular adaptation of omptins, we applied site-specific mutagenesis to make Epo of the plant pathogenic Erwinia pyrifoliae exhibit virulence-associated functions of its close homolog, the plasminogen activator Pla of Yersinia pestis. We addressed three virulence-associated functions exhibited by Pla, i.e., proteolytic activation of plasminogen, proteolytic degradation of serine protease inhibitors, and invasion into human cells. Results Pla and Epo expressed in Escherichia coli are both functional endopeptidases and cleave human serine protease inhibitors, but Epo failed to activate plasminogen and to mediate invasion into a human endothelial-like cell line. Swapping of ten amino acid residues at two surface loops of Pla and Epo introduced plasminogen activation capacity in Epo and inactivated the function in Pla. We also compared the structure of Pla and the modeled structure of Epo to analyze the structural variations that could rationalize the different proteolytic activities. Epo-expressing bacteria managed to invade human cells only after all extramembranous residues that differ between Pla and Epo and the first transmembrane β-strand had been changed. Conclusions We describe molecular adaptation of a protease from an environmental setting towards a virulence factor detrimental for humans. Our results stress the evolvability of bacterial β-barrel surface structures and the environment as a source of progenitor virulence molecules of human pathogens.

Published
2011
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