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1. VectorBase: a data resource for invertebrate vector genomics.

Author

Daniel Lawson, Peter Arensburger, Peter Atkinson, Nora J. Besansky, Robert V. Bruggner, Ryan Butler, Kathryn S. Campbell, George K. Christophides, Scott Christley, Emmanuel Dialynas, Martin Hammond, Catherine A. Hill, Nathan Konopinski, Neil F. Lobo, Robert M. MacCallum, Gregory R. Madey, Karine Megy, Jason Meyer, Seth Redmond, David W. Severson, Eric O. Stinson, Pantelis Topalis, Ewan Birney, William M. Gelbart, Fotis C. Kafatos, Christos Louis, and Frank H. Collins

Published
2009
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2. VectorBase: a home for invertebrate vectors of human pathogens.

Author

Daniel Lawson, Peter Arensburger, Peter Atkinson, Nora J. Besansky, Robert V. Bruggner, Ryan Butler, Kathryn S. Campbell, George K. Christophides, Scott Christley, Emmanuel Dialynas, David B. Emmert, Martin Hammond, Catherine A. Hill, Ryan C. Kennedy, Neil F. Lobo, Robert M. MacCallum, Gregory R. Madey, Karine Megy, Seth Redmond, Susan Russo, David W. Severson, Eric O. Stinson, Pantelis Topalis, Evgeni M. Zdobnov, Ewan Birney, William M. Gelbart, Fotis C. Kafatos, Christos Louis, and Frank H. Collins

Published
2007
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3. Genome sequence of Aedes aegypti, a major arbovirus vector

Author

Sergio Verjovski-Almeida, James E. Galagan, Ryan C. Kennedy, Zhiyong Xi, Jason R. Miller, Eric Eisenstadt, Kyanne R. Reidenbach, Robert V. Bruggner, Yu-Hui Rogers, Hadi Quesneville, Doreen Werner, Owen White, Alexander S. Raikhel, Mario Stanke, J. Spencer Johnston, Diane D. Lovin, Evgenia V. Kriventseva, Ian T. Paulsen, Kathryn S. Campbell, Norman H. Lee, Ewan Birney, Karyn Megy, Hean Koo, David Kulp, Shelby L. Bidwell, Jingsong Zhu, Philip Montgomery, Paolo Amedeo, Yongmei Zhao, Chinnappa D. Kodira, Javier Costas, Michael C. Schatz, Steven P. Sinkins, Claire M. Fraser-Liggett, Martin Shumway, Kurt LaButti, Akio Mori, Brendan J. Loftus, Manfred Grabherr, Eric O. Stinson, Frank H. Collins, Zhijian Jake Tu, Monique R. Coy, Matt Crawford, Janice P. Vanzee, William M. Gelbart, Joshua Orvis, Peter Arensburger, Chunhong Mao, Evgeny M. Zdobnov, Saul A. Kravitz, Suely Lopes Gomes, David DeCaprio, David G. Hogenkamp, Daniel Lawson, Dennis L. Knudson, David W. Severson, George Dimopoulos, Marcelo B. Soares, Sinéad B. O'Leary, Peter W. Atkinson, David M. Jaffe, Becky deBruyn, Martin Hammond, Ana L. T. O. Nascimento, Jim Biedler, Stefan Wyder, Jose M. C. Tubio, Bruce W. Birren, Catherine A. Hill, Chad Nusbaum, Eduardo Lee, Song Li, Susan E. Brown, Jennifer R. Wortman, James R. Hogan, Hamza El-Dorry, Qi Zhao, Linda Hannick, Carlos Frederico Martins Menck, Vishvanath Nene, Jonathan Crabtree, Steven L. Salzberg, Michael H. Holmes, Maria de Fatima Bonaldo, Quinghu Ren, Mihaela Pertea, Charles Roth, Evan Mauceli, Karin Eiglmeier, Horacio Naveira, Brian J. Haas, Qiandong Zeng, Neil F. Lobo, Jennifer R. Schneider, The Institute for Genomic Research, The Institute for Genomic Research, Rockville, European Bioinformatics Institute [Hinxton] ( EMBL-EBI ), European Molecular Biology Laboratory [Hinxton], Broad Institute of MIT and Harvard ( BROAD INSTITUTE ), Broad Institute of MIT and Harvard, Virginia Polytechnic Institute and State University [Blacksburg], University College Dublin [Dublin] ( UCD ), Bloomberg School of Public Health, Johns Hopkins University ( JHU ) -Bloomberg School of Public Health, University of Geneva Medical School, Swiss Institute of Bioinformatics-University of Geneva Medical School, University of Notre Dame ( UND ), Harvard University [Cambridge], College of Agricultural Sciences Colorado State University, Colorado State University [Fort Collins] ( CSU ) -College of Agricultural Sciences, Northwestern University [Evanston], University of California [Riverside] ( UCR ), Department of Atmospheric, Oceanic and Planetary Physics [Oxford] ( AOPP ), University of Oxford [Oxford], Purdue University [West Lafayette], Centro Nacional de Genotipado Fundación Pública Galega de Medicina Xenómica Hospital Clínico Universitario de Santiago, Centro Nacional de Genotipado-Fundación Pública Galega de Medicina Xenómica-Hospital Clínico Universitario de Santiago, Institut Pasteur [Paris], Universidade de Sao Paulo Instituto de Quimica, Universidade de São Paulo ( USP ) -Instituto de Quimica, Texas A&M University [College Station], Joint Technology Center, University of Massachusetts [Amherst] ( UMass Amherst ), Universidade de Sao Paulo, Institute of Biomedical Sciences, Universidade de São Paulo ( USP ) -Institute of Biomedical Sciences, Instituto Butantan [São Paulo], Universidade da Coruña, University of Maryland [College Park], Institut Jacques Monod ( IJM ), Université Paris Diderot - Paris 7 ( UPD7 ) -Centre National de la Recherche Scientifique ( CNRS ), University of California [Santa Cruz] ( UCSC ), Complexo Hospitalario Universitario de Santiago, Universität Göttingen, Georg-August-Universität Göttingen, George Washington University Medical Center, George Washington University ( GW ), The Institute for Genomic Research (TIGR), European Bioinformatics Institute [Hinxton] (EMBL-EBI), EMBL Heidelberg, Broad Institute of MIT and Harvard (BROAD INSTITUTE), Harvard Medical School [Boston] (HMS)-Massachusetts Institute of Technology (MIT)-Massachusetts General Hospital [Boston], University College Dublin [Dublin] (UCD), Johns Hopkins Bloomberg School of Public Health [Baltimore], Johns Hopkins University (JHU), Swiss Institute of Bioinformatics [Lausanne] (SIB), Université de Lausanne (UNIL)-Université de Lausanne (UNIL)-University of Geneva Medical School, University of Notre Dame [Indiana] (UND), Colorado State University [Fort Collins] (CSU)-College of Agricultural Sciences, University of California [Riverside] (UCR), University of California, Department of Atmospheric, Oceanic and Planetary Physics [Oxford] (AOPP), Universidade de São Paulo (USP)-Instituto de Quimica, University of Massachusetts [Amherst] (UMass Amherst), University of Massachusetts System (UMASS), Universidade de São Paulo (USP)-Institute of Biomedical Sciences (ICB/USP), Universidade de São Paulo (USP), University of Maryland System, Institut Jacques Monod (IJM (UMR_7592)), Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), University of California [Santa Cruz] (UCSC), Georg-August-University [Göttingen], The George Washington University (GW), George Washington University (GW), Université de Lausanne = University of Lausanne (UNIL)-Université de Lausanne = University of Lausanne (UNIL)-University of Geneva Medical School, Harvard University, University of California [Riverside] (UC Riverside), University of California (UC), University of Oxford, Institut Pasteur [Paris] (IP), Universidade de São Paulo = University of São Paulo (USP)-Instituto de Quimica, Universidade de São Paulo = University of São Paulo (USP)-Institute of Biomedical Sciences (ICB/USP), Universidade de São Paulo = University of São Paulo (USP), University of California [Santa Cruz] (UC Santa Cruz), Georg-August-University = Georg-August-Universität Göttingen, Zdobnov, Evgeny, and Wyder, Stefan

Subjects
0106 biological sciences, Male, Transcription, Genetic, Genome, Insect, transposons, receptors, Genes, Insect, Aedes/ genetics/metabolism, MESH: Genes, Insect, Yellow Fever/prevention & control/transmission, MESH: Base Sequence, 01 natural sciences, Dengue/prevention & control/transmission, MESH: Protein Structure, Tertiary, MESH: Arboviruses, MESH : Insect Vectors, MESH: Insect Proteins, MESH : Anopheles gambiae, MESH: Animals, MESH : Arboviruses, insects, MESH: Yellow Fever, superfamily, ddc:616, 0303 health sciences, Anopheles, MESH : Genes, Insect, 3. Good health, yellow-fever mosquito, anopheles-gambiae, drosophila-melanogaster, expression, evolution, organization, Drosophila melanogaster, MESH: DNA Transposable Elements, [ SDV.BBM.GTP ] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], Multigene Family, Public Health, MESH : Protein Structure, Tertiary, MESH: Sex Characteristics, Molecular Sequence Data, MESH : Multigene Family, MESH: Sex Determination (Genetics), MESH : Sex Determination (Genetics), Arbovirus, Article, 03 medical and health sciences, Species Specificity, [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], MESH: Anopheles gambiae, Yellow Fever, MESH: Species Specificity, Humans, MESH: Humans, MESH: Molecular Sequence Data, fungi, MESH : Humans, MESH : Sex Characteristics, Membrane Transport Proteins, Sex Determination Processes, medicine.disease, Insect Vectors, Protein Structure, Tertiary, Sex Determination (Genetics), MESH: Multigene Family, MESH: Female, MESH : Sequence Analysis, DNA, MESH: Sequence Analysis, DNA, Drosophila melanogaster/genetics, MESH : Molecular Sequence Data, Odorant binding, Insect Proteins/genetics, Anopheles gambiae, MESH: Dengue, Genome, MESH: Membrane Transport Proteins, Dengue, MESH : Membrane Transport Proteins, Aedes, Insect Vectors/ genetics/metabolism, MESH : Drosophila melanogaster, MESH : Female, Membrane Transport Proteins/genetics, Genetics, MESH : Insect Proteins, Sex Characteristics, Multidisciplinary, MESH: Synteny, MESH: Aedes, MESH : Genome, Insect, MESH : DNA Transposable Elements, Insect Proteins, Female, Orthologous Gene, MESH : Male, MESH : Dengue, Aedes aegypti, MESH: Insect Vectors, Biology, 010603 evolutionary biology, Synteny, MESH: Drosophila melanogaster, Protein Structure, Tertiary/genetics, MESH : Yellow Fever, parasitic diseases, medicine, MESH : Species Specificity, Animals, 030304 developmental biology, MESH : Aedes, Base Sequence, MESH: Genome, Insect, MESH: Transcription, Genetic, MESH : Synteny, MESH : Transcription, Genetic, Sequence Analysis, DNA, biology.organism_classification, MESH: Male, DNA Transposable Elements, MESH : Base Sequence, MESH : Animals, Arboviruses, Anopheles gambiae/genetics/metabolism
Abstract

We present a draft sequence of the genome of Aedes aegypti , the primary vector for yellow fever and dengue fever, which at ∼1376 million base pairs is about 5 times the size of the genome of the malaria vector Anopheles gambiae . Nearly 50% of the Ae. aegypti genome consists of transposable elements. These contribute to a factor of ∼4 to 6 increase in average gene length and in sizes of intergenic regions relative to An. gambiae and Drosophila melanogaster . Nonetheless, chromosomal synteny is generally maintained among all three insects, although conservation of orthologous gene order is higher (by a factor of ∼2) between the mosquito species than between either of them and the fruit fly. An increase in genes encoding odorant binding, cytochrome P450, and cuticle domains relative to An. gambiae suggests that members of these protein families underpin some of the biological differences between the two mosquito species.

Published
2016
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4. VectorBase: a data resource for invertebrate vector genomics

Author

William M. Gelbart, Fotis C. Kafatos, Robert V. Bruggner, Peter W. Atkinson, Ryan Butler, Nora J. Besansky, Karyn Megy, Scott Christley, Frank H. Collins, Peter Arensburger, Jason M. Meyer, Daniel Lawson, George K. Christophides, Robert M. MacCallum, Nathan Konopinski, Pantelis Topalis, Martin Hammond, Catherine A. Hill, Gregory R. Madey, Emmanuel Dialynas, Kathryn S. Campbell, Eric O. Stinson, David W. Severson, Christos Louis, Neil F. Lobo, Seth Redmond, and Ewan Birney

Subjects
Anopheles gambiae, 030231 tropical medicine, Genome, Insect, Genomics, Computational biology, Pediculus humanus, 03 medical and health sciences, 0302 clinical medicine, Aedes, parasitic diseases, Anopheles, Databases, Genetic, Genetics, Animals, 030304 developmental biology, 0303 health sciences, biology, Ixodes, Ecology, Gene Expression Profiling, Arthropod Vectors, Pediculus, Articles, biology.organism_classification, 3. Good health, Culex, Culicidae, Vocabulary, Controlled, Ixodes scapularis, Vector (epidemiology), Arthropod Vector
Abstract

VectorBase (http://www.vectorbase.org) is an NIAID-funded Bioinformatic Resource Center focused on invertebrate vectors of human pathogens. VectorBase annotates and curates vector genomes providing a web accessible integrated resource for the research community. Currently, VectorBase contains genome information for three mosquito species: Aedes aegypti, Anopheles gambiae and Culex quinquefasciatus, a body louse Pediculus humanus and a tick species Ixodes scapularis. Since our last report VectorBase has initiated a community annotation system, a microarray and gene expression repository and controlled vocabularies for anatomy and insecticide resistance. We have continued to develop both the software infrastructure and tools for interrogating the stored data.

Published
2008

5. Inactivation of pRB-Related Proteins p130 and p107 Mediated by the J Domain of Simian Virus 40 Large T Antigen

Author

Kathryn S. Campbell, Hilde Stubdal, Colleen Schweitzer, Juan Zalvide, James A. DeCaprio, and Thomas M. Roberts

Subjects
Proteasome Endopeptidase Complex, Antigens, Polyomavirus Transforming, Molecular Sequence Data, Mutant, Retinoblastoma-Like Protein p107, Biology, DNAJ Protein, Retinoblastoma Protein, Mice, Multienzyme Complexes, Tumor Cells, Cultured, Animals, Humans, Amino Acid Sequence, Phosphorylation, Nuclear protein, Molecular Biology, Peptide sequence, Heat-Shock Proteins, Binding Sites, Retinoblastoma-Like Protein p130, Retinoblastoma protein, Nuclear Proteins, Proteins, Cell Biology, HSP40 Heat-Shock Proteins, Phosphoproteins, Molecular biology, Growth Inhibitors, Cysteine Endopeptidases, embryonic structures, biology.protein, biological phenomena, cell phenomena, and immunity, Sequence Alignment, Research Article, Myc-tag
Abstract

Inactivation of the retinoblastoma tumor suppressor protein (pRB) contributes to tumorigenesis in a wide variety of cancers. In contrast, the role of the two pRB-related proteins, p130 and p107, in oncogenic transformation is unclear. The LXCXE domain of simian virus 40 large T antigen (TAg) specifically binds to pRB, p107, and p130. We have previously shown that the N terminus and the LXCXE domain of TAg cooperate to alter the phosphorylation state of p130 and p107. Here, we demonstrate that TAg promotes the degradation of p130 and that the N terminus of TAg is required for this activity. The N terminus of TAg has homology to the J domain of the DnaJ family of molecular chaperone proteins. Mutants with mutations in the J-domain homology region of TAg are defective for altering p130 and p107 phosphorylation and for p130 degradation. A heterologous J-domain from a human DnaJ protein can functionally substitute for the N terminus of TAg in the effect on p107 and p130 phosphorylation and p130 stability. We further demonstrate that the J-domain homology region of TAg confers a growth advantage to wild-type mouse embryo fibroblasts (MEFs) but is dispensable in the case of MEFs lacking both p130 and p107. This indicates that p107 and p130 have overlapping growth-suppressing activities whose inactivation is mediated by the J domain of TAg.

Published
1997
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6. Modulation of the Enzymatic Properties of Protein Phosphatase 2A Catalytic Subunit by the Recombinant 65-kDa Regulatory Subunit PR65alpha

Author

Bertrand Favre, Ned J.C. Lamb, Brian A. Hemmings, Kathryn S. Campbell, and Patric Turowski

Subjects
Protein Conformation, Protein subunit, Molecular Sequence Data, In Vitro Techniques, Spodoptera, Biology, Biochemistry, Cell Line, Substrate Specificity, law.invention, Protein structure, law, Escherichia coli, Phosphoprotein Phosphatases, Animals, Humans, Amino Acid Sequence, Protein Phosphatase 2, Binding site, Peptide sequence, chemistry.chemical_classification, Binding Sites, Protein phosphatase 2, Recombinant Proteins, Molecular Weight, A-site, Enzyme, chemistry, Mutagenesis, Site-Directed, Recombinant DNA, Rabbits, Baculoviridae, Dimerization
Abstract

All protein phosphatase 2A (PP2A) holoenzymes contain a 36-kDa catalytic subunit (PP2Ac) and a regulatory subunit of 65 kDa (PR65). We have studied the interaction between PP2Ac and PR65 in an in vitro system, using PP2Ac isolated from rabbit skeletal muscle and recombinant PR65alpha expressed in bacteria or insect cells. Bacterially expressed PR65alpha exhibited identical biochemical properties to the protein expressed and isolated from the baculoviral expression system. The association of recombinant PR65 with PP2Ac was very tight (K(D)app = 85 pM) and led to a suppression of PP2A activity, which was maximal (70-80%) when phosphoproteins were used as substrates. When less-structured or smaller substrates (such as phosphopeptides) were used, this inhibition was only 30%. PR65 stimulated PP2Ac activity when the assays were performed in the presence of polycations. This indicates that the PR65 not only serves the previously predicted structural role as a molecular scaffold, but also allosterically modulates the enzymatic properties of PP2Ac. Furthermore, we identified a site of interaction between PP2Ac and PR65alpha by disruption of a stretch of basic amino acids by introduction of a glutamate at position 416. This produced an almost 100-fold reduced affinity for PP2Ac and indicated that this basic motif is an important determinant for the interaction of PR65 and PP2Ac.

Published
1997
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7. DnaJ/hsp40 chaperone domain of SV40 large T antigen promotes efficient viral DNA replication

Author

Karen P. Mullane, Kathryn S. Campbell, Juan Zalvide, James A. DeCaprio, Brian Schaffhausen, James M. Pipas, Pamela A. Silver, Thomas M. Roberts, I A Aksoy, and Hilde Stubdal

Subjects
DNA Replication, Antigens, Polyomavirus Transforming, Recombinant Fusion Proteins, Molecular Sequence Data, Eukaryotic DNA replication, Simian virus 40, Virus Replication, DNAJ Protein, Cell Line, DNA replication factor CDT1, Replication factor C, SeqA protein domain, Control of chromosome duplication, Genetics, Animals, Humans, HSP70 Heat-Shock Proteins, Amino Acid Sequence, Heat-Shock Proteins, DNA Primers, Base Sequence, Molecular Structure, Sequence Homology, Amino Acid, biology, Escherichia coli Proteins, HSC70 Heat-Shock Proteins, DNA replication, HSP40 Heat-Shock Proteins, Mutation, biology.protein, Origin recognition complex, Carrier Proteins, Developmental Biology
Abstract

The amino-terminal domain of SV40 large tumor antigen (TAg) is required for efficient viral DNA replication. However, the biochemical activity associated with this domain has remained obscure. We show here that the amino-terminal domain of TAg shares functional homology with the J-domain of DnaJ/hsp40 molecular chaperones. DnaJ proteins function as cofactors by regulating the activity of a member of the 70-kD heat shock protein family. Genetic analyses demonstrated that amino-terminal sequences of TAg comprise a novel J-domain that mediates a specific interaction with the constitutively expressed hsc70 and show that the J-domain is also required for efficient viral DNA replication in vivo. Furthermore, we demonstrated that the J-domain of two human DnaJ homologs, HSJ1 or DNAJ2, could substitute functionally for the amino-terminus of TAg in promoting viral DNA replication. Together, our findings suggest that TAg uses its J-domain to support SV40 DNA replication in a manner that is strikingly similar to the use of Escherichia coli DnaJ by bacteriophage lambda in DNA replication. However, TAg has evolved a more efficient strategy of DNA replication through an intrinsic J-domain to associate directly with a partner chaperone protein. Our observations provide evidence of a role for chaperone proteins in the process of eukaryotic DNA replication.

Published
1997
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8. Identification of regions in polyomavirus middle T and small t antigens important for association with protein phosphatase 2A

Author

B A Hemmings, Kathryn S. Campbell, Thomas M. Roberts, David C. Pallas, and Kurt R. Auger

Subjects
Immunoprecipitation, Antigens, Polyomavirus Transforming, Molecular Sequence Data, Proto-Oncogene Proteins pp60(c-src), Immunology, Mutant, macromolecular substances, Plasma protein binding, Biology, medicine.disease_cause, Microbiology, Mice, Phosphatidylinositol 3-Kinases, Antigen, Virology, Phosphoprotein Phosphatases, medicine, Animals, Amino Acid Sequence, Protein Phosphatase 2, Peptide sequence, Cell Line, Transformed, DNA Primers, chemistry.chemical_classification, Mice, Inbred BALB C, Mutation, Base Sequence, 3T3 Cells, Protein phosphatase 2, Molecular biology, Amino acid, Phosphotransferases (Alcohol Group Acceptor), chemistry, Insect Science, embryonic structures, Research Article, Protein Binding
Abstract

Two subunits of protein phosphatase 2A (PP2A) have been shown previously to bind to the small t and middle T antigens (ST and MT, respectively) of polyomavirus. To determine sequences important for binding of PP2A to ST and MT, we first constructed a series of ST mutants in regions known to be important for biological activity of ST and MT. Several mutations in two small regions just amino terminal to the Cys-X-Cys-X-X-Cys motifs of ST and MT abolished PP2A binding to ST in vitro. Parallel mutations were constructed in MT to investigate the role of PP2A binding in the function of polyomavirus MT. Wild-type and mutant MT proteins were stably expressed in NIH 3T3 cells and analyzed (i) for their ability to induce transformation and (ii) for associated cellular proteins and corresponding enzymatic activities previously described as associating with wild-type MT. A number of the mutant MTs were found to be defective in binding of PP2A as assayed by coimmunoprecipitation. In contrast, a deletion of the highly conserved stretch of amino acids 42 to 47 (His-Pro-Asp-Lys-Gly-Gly) in the ST-MT-large T antigen common region did not affect PP2A binding to MT. MT mutants defective for PP2A binding were also defective in transformation, providing further evidence that association with PP2A is important for the ability of MT to transform cells. All mutants which were impaired for PP2A binding were similarly or more dramatically impaired for associated protein and lipid kinase activities, supporting the possibility that PP2A binding is necessary for the formation and/or stability of an MT-pp60c-src complex.

Published
1995
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9. Polyoma middle tumor antigen interacts with SHC protein via the NPTY (Asn-Pro-Thr-Tyr) motif in middle tumor antigen

Author

Egon Ogris, Thomas M. Roberts, Brian J. Druker, Kurt R. Auger, Brenda Burke, Brian Schaffhausen, Wen Su, David C. Pallas, and Kathryn S. Campbell

Subjects
Src Homology 2 Domain-Containing, Transforming Protein 1, Antigens, Polyomavirus Transforming, Protein subunit, Molecular Sequence Data, Biology, SRC Family Tyrosine Kinase, environment and public health, Mice, Proto-Oncogenes, Animals, Humans, Amino Acid Sequence, Tyrosine, Kinase activity, Adaptor Proteins, Signal Transducing, GRB2 Adaptor Protein, Oncogene Proteins, Binding Sites, Multidisciplinary, Sequence Homology, Amino Acid, Proteins, 3T3 Cells, Molecular biology, Clone Cells, ErbB Receptors, Adaptor Proteins, Vesicular Transport, Shc Signaling Adaptor Proteins, Mutagenesis, Site-Directed, biology.protein, Phosphorylation, GRB2, biological phenomena, cell phenomena, and immunity, hormones, hormone substitutes, and hormone antagonists, Research Article, Proto-oncogene tyrosine-protein kinase Src
Abstract

Polyomavirus middle tumor antigen (MT) transforms a large number of cell types by binding to and modulating the activities of cellular proteins. Previous genetic analysis defined in MT an independent motif, NPTY (Asn-Pro-Thr-Tyr), required for transformation. This report demonstrates that NPTY is required for interaction between MT and SHC protein, a Src homology 2 (SH2)-containing protooncogene product implicated in activating Ras via association with GRB2 protein. SHC is phosphorylated on tyrosine and associates with GRB2 in MT-transformed cells. These effects require an intact NPTY motif in MT. SHC immunoprecipitates from MT-transformed cells possess kinase activity that phosphorylates not only SHC and MT but also the 85-kDa subunit of phosphatidylinositol 3-kinase. This result suggests that a complex exists that contains, at a minimum, MT, Src family tyrosine kinases, phosphatidylinositol 3-kinase, and SHC.

Published
1994
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10. VectorBase: a home for invertebrate vectors of human pathogens

Author

Seth Redmond, Robert V. Bruggner, Evgeni M. Zdobnov, Karyn Megy, Fotis C. Kafatos, Emmanuel Dialynas, David W. Severson, Kathryn S. Campbell, Susan M. Russo, Ryan C. Kennedy, David B. Emmert, Ewan Birney, Scott Christley, Pantelis Topalis, Nora J. Besansky, George K. Christophides, Frank H. Collins, Neil F. Lobo, Peter Arensburger, Ryan Butler, Eric O. Stinson, Peter W. Atkinson, Catherine A. Hill, Gregory R. Madey, Martin Hammond, Christos Louis, William M. Gelbart, Daniel Lawson, and Robert M. MacCallum

Subjects
Anopheles gambiae, 030231 tropical medicine, Genome, Insect, Aedes aegypti, Dengue fever, 03 medical and health sciences, User-Computer Interface, 0302 clinical medicine, Aedes, Anopheles, parasitic diseases, Databases, Genetic, Genetics, medicine, Animals, Humans, Conserved Sequence, 030304 developmental biology, ddc:616, 0303 health sciences, Internet, biology, Base Sequence, Insect Vectors/ genetics, Yellow fever, Articles, Aedes/ genetics, Genomics, medicine.disease, biology.organism_classification, Virology, Insect Vectors, 3. Good health, Vector (epidemiology), Anopheles gambiae/ genetics, Malaria
Abstract

VectorBase (http://www.vectorbase.org/) is a web-accessible data repository for information about invertebrate vectors of human pathogens. VectorBase annotates and maintains vector genomes providing an integrated resource for the research community. Currently, VectorBase contains genome information for two organisms: Anopheles gambiae, a vector for the Plasmodium protozoan agent causing malaria, and Aedes aegypti, a vector for the flaviviral agents causing Yellow fever and Dengue fever.

Published
2007

11. Insights into social insects from the genome of the honeybee Apis mellifera

Author

George M. Weinstock, Andrew K. Jones, Katherine A Aronstein, Irene Gattermeier, Kiyoshi Kimura, Susan E. Fahrbach, Laura I. Decanini, Christina M. Grozinger, Evgeny M. Zdobnov, Susan J. Brown, Jonathan V. Sweedler, Kazutoyo Osoegawa, Christian A. Ross, Joseph J. Gillespie, Ngoc Nguyen, Geert Baggerman, Frank Hauser, Dan Graur, Michelle M. Elekonich, Alison R. Mercer, Amanda F. Svatek, Jean Marie Cornuet, Cornelis J. P. Grimmelikhuijzen, Aleksandar Milosavljevic, Anand Venkatraman, Andrew J. Schroeder, Huaiyang Jiang, Michael R. Kanost, Justin T. Reese, Margaret Morgan, Tomoko Fujiyuki, Kim C. Worley, Susanta K. Behura, Jun Kawai, Robert Kucharski, Gildardo Aquino-Perez, Miguel Corona, Diana E. Wheeler, Kathryn S. Campbell, William M. Gelbart, Amy L. Toth, Yanping Chen, Mira Cohen, Noam Kaplan, Michihira Tagami, Miguel A. Peinado, Peter K. Dearden, Glenford Savery, Liliane Schoofs, Takeo Kubo, Giuseppe Cazzamali, Sylvain Forêt, Thomas C. Newman, Ross Overbeek, Piero Carninci, Ryszard Maleszka, Barbara J. Ruef, Michal Linial, Alexandre S. Cristino, Mary A. Schuler, Huyen Dinh, J. Troy Littleton, Manoj P. Samanta, Waraporn Tongprasit, L. Sian Grametes, Eran Elhaik, Jean-Luc Imler, Zhen Zou, Rodrigo A. Velarde, Tanja Gempe, Dorothea Eisenhardt, Juan Manuel Anzola, Graham J. Thompson, Aaron J. Mackey, René Feyereisen, Mrcia M.G. Bitondi, Lora Lewis, Guy Bloch, Richard A. Gibbs, Jane Peterson, Jay D. Evans, Robert E. Page, Amanda B. Hummon, Viktor Stolc, Donna M. Muzny, Yair Shemesh, Francis M. F. Nunes, Dawn Lopez, Judith H. Willis, Martin Hasselmann, Mark S. Guyer, John G. Oakeshott, Pinglei Zhou, Eriko Kage, Dominique Vautrin, Kevin J. Hackett, Sandra L. Lee, Clay Davis, Christine Emore, Gene E. Robinson, Alexandre Souvorov, T.A. Richmond, Rachel Thorn, Jurgen Huybrechts, Elad B. Rubin, Craig Mizzen, Deborah R. Smith, Walter S. Sheppard, Takekazu Kunieda, Adam Felsenfeld, Bingshan Li, Jeffrey G. Reid, La Ronda Jackson, Jamie J. Cannone, Robin R. Gutell, Jireh Santibanez, Megan J. Wilson, David B. Sattelle, Azusa Kamikouchi, George Miner, Hideaki Takeuchi, Geoffrey Okwuonu, Jennifer Hume, Jonathan Miller, Kazuaki Ohashi, Angela Jovilet, Yoshihide Hayashizaki, Joseph Chacko, Paul Kitts, Erica Sodergren, Charles Hetru, Andrew V. Suarez, Brian P. Lazzaro, Susan E. St. Pierre, Evy Vierstraete, Haobo Jiang, Sandra Hines, Teresa D. Shippy, Greg J. Hunt, Peter Kosarev, Dan Hultmark, Stefan Albert, Susan M. Russo, Chung Li Shu, Michel Solignac, H. Michael G. Lattorff, Xu Ling, Grard Leboulle, Miklós Csürös, Neil D. Tsutsui, Lynne V. Nazareth, Ying Wang, Florence Mougel, Beverly B. Matthews, Kevin L. Childs, Rita A. Wright, Hugh M. Robertson, Lan Zhang, Peter Verleyen, Daniel B. Weaver, Christie Kovar, Chikatoshi Kai, Charles W. Whitfield, Madeline A. Crosby, Natalia V. Milshina, Reed M. Johnson, Michael A. Ewing, Peter L. Jones, Sandra L. Rodriguez-Zas, Michael B. Eisen, Klaus Hartfelder, Karl H.J. Gordon, W. Augustine Dunn, Ling Ling Pu, M. Monnerot, Stephen Richards, Richa Agarwala, Judith Hernandez, Pieter J. de Jong, Michael Williamson, Marcé D. Lorenzen, Zilá Luz Paulino Simões, Mark D. Drapeau, Donna Villasana, Katarína Bíliková, J. Spencer Johnston, David I. Schlipalius, Xuehong Wei, Laurent Duret, Venky N. Iyer, Andrew G. Clark, Christine G. Elsik, Hilary Ranson, Kyle T. Beggs, Mireia Jordà, Shiro Fukuda, Seth A. Ament, Vivek Iyer, Jozef Šimúth, Stewart H. Berlocher, May R. Berenbaum, Robin F. A. Moritz, Tatsuhiko Kadowaki, Charles Claudianos, Gro V. Amdam, Yue Liu, Naoko Sakazume, Morten Schioett, Paul Havlak, Anita M. Collins, Dirk C. de Graaf, Derek Collinge, Ivica Letunic, Carlos H. Lobo, Mizue Morioka, Martin Beye, Rachel Gill, C. Michael Dickens, Daisuke Sasaki, Victor V. Solovyev, Peer Bork, Sunita Biswas, David A. Wheeler, Heidi Paul, Bioinformatique, phylogénie et génomique évolutive (BPGE), Département PEGASE [LBBE] (PEGASE), Laboratoire de Biométrie et Biologie Evolutive - UMR 5558 (LBBE), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de Recherche en Informatique et en Automatique (Inria)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de Recherche en Informatique et en Automatique (Inria)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Centre National de la Recherche Scientifique (CNRS)-Laboratoire de Biométrie et Biologie Evolutive - UMR 5558 (LBBE), Université de Lyon-Université de Lyon-Institut National de Recherche en Informatique et en Automatique (Inria)-VetAgro Sup - Institut national d'enseignement supérieur et de recherche en alimentation, santé animale, sciences agronomiques et de l'environnement (VAS)-Centre National de la Recherche Scientifique (CNRS), Laboratoire Evolution, Génomes et Spéciation (LEGS), Centre National de la Recherche Scientifique (CNRS), and Physical and genetic mapping

Subjects
Male, 0106 biological sciences, Transposable element, [SDV.OT]Life Sciences [q-bio]/Other [q-bio.OT], Proteome, Genome, Insect, Molecular Sequence Data, Genes, Insect, Genomics, Biology, 010603 evolutionary biology, 01 natural sciences, Genome, Article, Evolution, Molecular, 03 medical and health sciences, Molecular evolution, Phylogenetics, Animals, Gene, Phylogeny, abeille domestique, 030304 developmental biology, Whole genome sequencing, Genetics, Base Composition, 0303 health sciences, [SDV.GEN]Life Sciences [q-bio]/Genetics, Multidisciplinary, Behavior, Animal, Reproduction, SOCIAL BEHAVIOR, [SDV.BA]Life Sciences [q-bio]/Animal biology, Immunity, APIS MELLIFERA, food and beverages, Bees, Telomere, Physical Chromosome Mapping, INSECTE, Gene Expression Regulation, DNA methylation, DNA Transposable Elements, Female, GENETIQUE DES POPULATIONS, Signal Transduction
Abstract

Ce travail résulte de la collaboration de très nombreux chercheurs. Seuls les auteurs de la rubrique Physical and Genetic Mapping sont cités explicitement.; Here we report the genome sequence of the honeybee Apis mellifera, a key model for social behaviour and essential to global ecology through pollination. Compared with other sequenced insect genomes, the A. mellifera genome has high A1T and CpG contents, lacks major transposon families, evolves more slowly, and is more similar to vertebrates for circadian rhythm, RNA interference and DNA methylation genes, among others. Furthermore, A.mellifera has fewer genes for innate immunity, detoxification enzymes, cuticle-forming proteins and gustatory receptors, more genes for odorant receptors, and novel genes for nectar and pollen utilization, consistent with its ecology and social organization. Compared to Drosophila, genes in early developmental pathways differ in Apis, whereas similarities exist for functions that differ markedly, such as sex determination, brain function and behaviour. Population genetics suggests a novel African origin for the species A.mellifera and insights into whether Africanized bees spread throughout the New World via hybridization or displacement

Published
2006
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12. [Untitled]

Author

Christopher D. Smith, Yanmei Huang, Eleanor J Whitfield, William M. Gelbart, Bettencourt Brian, Beverley B. Matthews, Suzanna E. Lewis, Madeline A. Crosby, Gillian Millburn, Aubrey D.N.J. de Grey, Pavel Hradecky, Sima Misra, Christopher J. Mungall, Rachel Drysdale, Susan E. Celniker, Simon Prochnik, ShengQiang Shu, Andrew J. Schroeder, Mark Stapleton, Chihiro Yamada, Jonathan L. Tupy, Gerald M. Rubin, Leyla Bayraktaroglu, J. Richter, Nomi L. Harris, Benjamin P. Berman, Michael Ashburner, Joshua S. Kaminker, Kathryn S. Campbell, and Susan M. Russo

Subjects
Transposable element, Regulation of gene expression, Genetics, 0303 health sciences, biology, biology.organism_classification, Genome, 03 medical and health sciences, Nested gene, 0302 clinical medicine, Drosophila melanogaster, FlyBase : A Database of Drosophila Genes & Genomes, Gene, 030217 neurology & neurosurgery, Drosophila Protein, 030304 developmental biology
Abstract

Background: The recent completion of the Drosophila melanogaster genomic sequence to high quality and the availability of a greatly expanded set of Drosophila cDNA sequences, aligning to 78% of the predicted euchromatic genes, afforded FlyBase the opportunity to significantly improve genomic annotations. We made the annotation process more rigorous by inspecting each gene visually, utilizing a comprehensive set of curation rules, requiring traceable evidence for each gene model, and comparing each predicted peptide to SWISS-PROT and TrEMBL sequences. Results: Although the number of predicted protein-coding genes in Drosophila remains essentially unchanged, the revised annotation significantly improves gene models, resulting in structural changes to 85% of the transcripts and 45% of the predicted proteins. We annotated transposable elements and non-protein-coding RNAs as new features, and extended the annotation of untranslated (UTR) sequences and alternative transcripts to include more than 70% and 20% of genes, respectively. Finally, cDNA sequence provided evidence for dicistronic transcripts, neighboring genes with overlapping UTRs on the same DNA sequence strand, alternatively spliced genes that encode distinct, non-overlapping peptides, and numerous nested genes. Conclusions: Identification of so many unusual gene models not only suggests that some mechanisms for gene regulation are more prevalent than previously believed, but also underscores the complex challenges of eukaryotic gene prediction. At present, experimental data and human curation remain essential to generate high-quality genome annotations.

Published
2002
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14. Structure in theGisla: Undinna � �ttir

Author

Kathryn S. Campbell

Subjects
Structure (mathematical logic), Linguistics and Language, Philology, Literature and Literary Theory, Philosophy, Comparative literature, Historical linguistics, Comparative linguistics, Syntax, Linguistics
Published
1986
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15. Role of the HTLV-III/LAV envelope in syncytium formation and cytopathicity

Author

William A. Haseltine, Kathryn S. Campbell, Wei Chun Goh, Craig A. Rosen, and Joseph Sodroski

Subjects
Antigens, Differentiation, T-Lymphocyte, Genes, Viral, viruses, Biology, Transfection, Deltaretrovirus, Virus, Cell Fusion, Viral envelope, Cell–cell interaction, Cytopathogenic Effect, Viral, Viral Envelope Proteins, Cytotoxic T cell, Humans, Cytopathic effect, Glycoproteins, Syncytium, Acquired Immunodeficiency Syndrome, Multidisciplinary, Cell fusion, Immune Sera, Antibodies, Monoclonal, Virology, Cell culture, Antigens, Surface, Plasmids
Abstract

Acquired immune deficiency syndrome (AIDS) is characterized by marked depletion of the T4+ helper subset of T cells. The aetiological agent of the disease, the human T-lymphotropic virus type III (HTLV-III)/lymphadenopathy-associated virus (LAV), specifically kills T4+ cells in vitro. Part of this specificity for the T4+ population residues in the relative efficiency with which HTLV-III infects these cells, as a result of a specific interaction between the T4 molecule and the virus envelope glycoprotein. In addition, the cytotoxic consequences of HTLV-III replication are dependent on cell type, as certain lymphoid and myeloid cells can be productively infected without notable cytopathic effect. Here we investigate the basis for the specific cytotoxicity of the virus, and report that high-level expression of the HTLV-III envelope gene induces syncytia and concomitant cell death in T4+ cell lines but not in a B-lymphocyte line. Syncytium formation depends on the interaction of envelope-expressing cells with neighbouring cells bearing surface T4 molecules. These results explain, at least in part, the specific cytopathic effect of HTLV-III infections.

Published
1986

16. Vitamin C Treatment in Lead Poisoning

Author

Kathryn S. Campbell, Edward J. Amberg, and Harry N. Holmes

Subjects
medicine.medical_specialty, Blood picture, Multidisciplinary, Vitamin C, business.industry, Scurvy, medicine.disease, Ascorbic acid, Gastroenterology, Lead poisoning, Endocrinology, Internal medicine, medicine, business
Published
1939
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