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Coiled coils appear in countless structural contexts, as appendages to small proteins, as parts of multi-domain proteins, and as building blocks of filaments. Although their structure is unpretentious and their basic properties are understood in great detail, the spectrum of functional properties they provide in different proteins has become increasingly complex. This chapter aims to depict this functional spectrum, to identify common themes and their molecular basis, with an emphasis on new insights gained into dynamic aspects.

Poultry is the first source of animal protein for human consumption. In a changing world, this sector is facing new challenges, such as a projected increase in demand, higher standards of food quality and safety, and reduction of environmental impact. Chicken coccidiosis is a highly widespread enteric disease caused by Eimeria spp. which causes significant economic losses to the poultry industry worldwide; however, the impact on family poultry holders or backyard production—which plays a key role in food security in small communities and involves mainly rural women—has been little explored. Coccidiosis disease is controlled by good husbandry measures, chemoprophylaxis, and/or live vaccination. The first live vaccines against chicken coccidiosis were developed in the 1950s; however, after more than seven decades, none has reached the market. Current limitations on their use have led to research in next-generation vaccines based on recombinant or live-vectored vaccines. Next-generation vaccines are required to control this complex parasitic disease, and for this purpose, protective antigens need to be identified. In this review, we have scrutinised surface proteins identified so far in Eimeria spp. affecting chickens. Most of these surface proteins are anchored to the parasite membrane by a glycosylphosphatidylinositol (GPI) molecule. The biosynthesis of GPIs, as well as the role of currently identified surface proteins and interest as vaccine candidates has been summarised. The potential role of surface proteins in drug resistance and immune escape and how these could limit the efficacy of control strategies was also discussed. [ABSTRACT FROM AUTHOR]

The highly contagious SARS‐CoV‐2 and its associated disease (COVID‐19) are a threat to global public health and economies. To develop effective treatments for COVID‐19, we must understand the host cell types, cell states and regulators associated with infection and pathogenesis such as dysregulated transcription factors (TFs) and surface proteins, including signaling receptors. To link cell surface proteins with TFs, we recently developed SPaRTAN (Single‐cell Proteomic and RNA‐based Transcription factor Activity Network) by integrating parallel single‐cell proteomic and transcriptomic data based on Cellular Indexing of Transcriptomes and Epitopes by sequencing (CITE‐seq) and gene cis‐regulatory information. We apply SPaRTAN to CITE‐seq data sets from patients with varying degrees of COVID‐19 severity and healthy controls to identify the associations between surface proteins and TFs in host immune cells. Here, we present COVID‐19db of Immune Cell States (https://covid19db.streamlit.app/), a web server containing cell surface protein expression, SPaRTAN‐inferred TF activities, and their associations with major host immune cell types. The data include four high‐quality COVID‐19 CITE‐seq data sets with a toolset for user‐friendly data analysis and visualization. We provide interactive surface protein and TF visualizations across major immune cell types for each data set, allowing comparison between various patient severity groups for the discovery of potential therapeutic targets and diagnostic biomarkers. [ABSTRACT FROM AUTHOR]

The cell surface proteins of gram-positive bacteria are involved in many important biological functions, including the infection of host cells. Owing to their virulent nature, these proteins are also considered strong candidates for potential drug or vaccine targets. Among the various cell surface proteins of gram-positive bacteria, LPXTG-like proteins form a major class. These proteins have a highly conserved C-terminal cell wall sorting signal, which consists of an LPXTG sequence motif, a hydrophobic domain, and a positively charged tail. These surface proteins are targeted to the cell envelope by a sortase enzyme via transpeptidation. A variety of LPXTG-like proteins have been experimentally characterized; however, their number in public databases has increased owing to extensive bacterial genome sequencing without proper annotation. In the absence of experimental characterization, identifying and annotating these sequences is extremely challenging. Therefore, in this study, we developed the first machine learning-based predictor called GPApred, which can identify LPXTG-like proteins from their primary sequences. Using a newly constructed benchmark dataset, we explored different classifiers and five feature encodings and their hybrids. Optimal features were derived using the recursive feature elimination method, and these features were then trained using a support vector machine algorithm. The performance of different models was evaluated using independent datasets, and a final model (GPApred) was selected based on consistency during cross-validation and independent assessment. GPApred can be an effective tool for predicting LPXTG-like sequences and can be further employed for functional characterization or drug targeting. Availability: https://procarb.org/gpapred/. [ABSTRACT FROM AUTHOR]

Background: Group B Streptococcus (GBS) transmission during pregnancy causes preterm labor, stillbirths, fetal injury, or neonatal infections. Rates of adult infections are also rising. The GBS-NN vaccine, engineered by fusing N-terminal domains of GBS Alpha C and Rib proteins, is safe in healthy, nonpregnant women, but further assessment is needed for use during pregnancy. Here, we tested GBS-NN vaccine efficacy using mouse models that recapitulate human GBS infection outcomes.Methods: Following administration of GBS-NN vaccine or adjuvant, antibody profiles were compared by ELISA. Vaccine efficacy was examined by comparing infection outcomes in GBS-NN vaccinated versus adjuvant controls during systemic and pregnancy-associated infections, and during intranasal infection of neonatal mice following maternal vaccination.Results: Vaccinated mice had higher GBS-NN-specific IgG titers versus controls. These antibodies bound alpha C and Rib on GBS clinical isolates. Fewer GBS were recovered from systemically challenged vaccinated mice versus controls. Although vaccination did not eliminate GBS during ascending infection in pregnancy, vaccinated dams experienced fewer in utero fetal deaths. Additionally, maternal vaccination prolonged neonatal survival following intranasal GBS challenge.Conclusions: These findings demonstrate GBS-NN vaccine efficacy in murine systemic and perinatal GBS infections and suggest that maternal vaccination facilitates the transfer of protective antibodies to neonates. [ABSTRACT FROM AUTHOR]

The Gram-positive bacterium Listeria monocytogenes is an important pathogen that causes a foodborne illness with a high percentage of fatalities. Surface proteins, specifically expressed from a wide range of L. monocytogenes serotypes under selective enrichment culture conditions, can serve as targets for the detection and isolation of this pathogen using antibody-based methods. Among a number of surface proteins identified by mass spectrometry in a previous proteomic study, six candidates (annotated as LMOf2365_0148, LMOf2365_0312, LMOf2365_0546, LMOf2365_1883, LMOf2365_ 2111, and LMOf2365_2742) were selected here for investigating their expression in the bacterial cells cultured in vitro by raising rabbit polyclonal antibodies (PAbs) against the recombinant form of each candidate. These protein candidates contained regions conserved among various L. monocytogenes isolates but variable in other Listeria species. LMOf2365_0148, an uncharacterized protein with a LPXTG motif accountable for covalent linkage to the cell wall peptidoglycan, exhibited a strong reaction signal from anti-LMOf2365_0148 PAb binding to the cell surface, as detected by immunofluorescence microscopy. Further study, through the generation of a panel of mouse monoclonal antibodies (MAbs) to the recombinant LMOf2365_0148, showed that one of the MAbs, M3686, reacted to bacterial isolates belonging to all three lineages of L. monocytogenes under Health Canada's standard enrichment culture conditions (MFHPB-07 and MFHPB-30). These results demonstrated the potential of using LMOf2365_0148 as a surface biomarker, in conjunction with specific MAbs developed here, for the isolation and detection of L. monocytogenes from foods and food processing environments. [ABSTRACT FROM AUTHOR]

• Removing SGSPs/SGAPs resulted in poor bread quality. • It decreased the specific volume and crumb porosity in bread. • Bread without SGSPs modified the water migration and distribution. • More soluble starch leached and promoted relative recrystallinity. The influence of starch granule surface proteins (SGSPs) and starch granule-associated proteins (SGAPs) on bread retrogradation was investigated in a reconstituted dough system. The removal of both SGSPs and SGAPs resulted in poor bread qualities, decreasing specific volume and crumb porosity, leading to more baking loss and compact crumb structure. Particularly, removing SGSPs was effective in promoting the bread retrogradation. After 7 days of storage, the hardness of bread without SGSPs showed an increase of 353.34 g than the bread without SGAPs. Proton population and relaxation times exhibited that the absence of SGSPs significantly decreased the content of bound water from 11.51 % to 7.03 %, indicating lower water-holding capacity due to the loosen gelling structure. Compared to the control group, bread without SGSPs accelerated the starch recrystallinity by a reduction in soluble starch content, thereby increasing the retrogradation enthalpy and relative crystallinity through promoting the molecular reassociation in starch. [ABSTRACT FROM AUTHOR]

Malaria has remained a major health concern for decades among people living in tropical and sub-tropical countries. Plasmodium falciparum is one of the critical species that cause severe malaria and is responsible for major mortality. Moreover, the parasite has generated resistance against all WHO recommended drugs and therapies. Therefore, there is an urgent need for preventive measures in the form of reliable vaccines to achieve the target of a malaria-free world. Surface proteins are the preferable choice for subunit vaccine development because they are rapidly detected and engaged by host immune cells and vaccination-induced antibodies. Additionally, abundant surface or membrane proteins may contribute to the opsonization of pathogens by vaccine-induced antibodies. In our study, we have listed all those surface proteins from the literature that could be functionally important and essential for infection and immune evasion of the malaria parasite. Eight Plasmodium surface and membrane proteins from the pre-erythrocyte and erythrocyte stages were shortlisted. Thirty-seven epitopes (B-cell, CTL, and HTL epitopes) from these proteins were predicted using immune-informatic tools and joined with suitable peptide linkers to design a vaccine construct. A TLR-4 agonist peptide adjuvant was added at the N-terminus of the multi-epitope series, followed by the PADRE sequence and EAAAK linker. The TLR-4 receptor was docked with the construct's anticipated model structure. The complex of vaccine and TLR-4, with the lowest energy −1514, was found to be stable under simulated physiological settings. This study has provided a novel multi-epitope construct that may be exploited further for the development of an efficient vaccine for malaria. [ABSTRACT FROM AUTHOR]

Leptospira , a zoonotic pathogen, is known to infect various hosts and can establish persistent infection. This remarkable ability of bacteria is attributed to its potential to modulate (activate or evade) the host immune response by exploiting its surface proteins. We have identified and characterized the domain of the variable region of Leptospira immunoglobulin-like protein A (LAV) involved in immune modulation. The 11th domain (A11) of the variable region of LigA (LAV) induces a strong TLR4 dependent innate response leading to subsequent induction of humoral and cellular immune responses in mice. A11 is also involved in acquiring complement regulator FH and binds to host protease Plasminogen (PLG), there by mediating functional activity to escape from complement-mediated killing. The deletion of A11 domain significantly impaired TLR4 signaling and subsequent reduction in the innate and adaptive immune response. It also inhibited the binding of FH and PLG thereby mediating killing of bacteria. Our study discovered an unprecedented role of LAV as a nuclease capable of degrading Neutrophil Extracellular Traps (NETs). This nuclease activity was primarily mediated by A11. These results highlighted the moonlighting function of LigA and demonstrated that a single domain of a surface protein is involved in modulating the host innate immune defenses, which might allow the persistence of Leptospira in different hosts for a long term without clearance. [ABSTRACT FROM AUTHOR]

The increase in concern from viable cells of probiotics specifically in acute inflammatory conditions has led to the emergence of the concept of postbiotics as a safer alternative therapy in the field of health and wellness. The aim of the present study was to evaluate the efficacy of surface proteins from three probiotic strains in dextran sodium sulfate and trinitrobenzenesulphonic acid = induced colitis mouse models. The molecular weight of total surface proteins extracted from the three probiotic strains ranged from ∼25 to ∼250 kDa with the presence of negligible levels of endotoxins. Surface layer proteins (SLPs) (∼45 kDa) were found to be present only in the Lactobacillus acidophilus NCFM strain. In the in vivo study, significant differences were not observed in the weight loss and general appetite, however, the decrease in colon length was apparent in TNBS colitis control mice. Further, the administration of these surface proteins significantly reversed the histopathological damages induced by the colitogens and improved the overall histological score. The oral ingestion of these surface proteins also led to a decrease in myeloperoxidase activity and TNF-α expression while the IL-10 levels significantly increased for the strain NCFM followed by MTCC 5690 and MTCC 5689. Overall, the present study signifies the ameliorative role of probiotic surface proteins in colitis mice, thereby, offering a potential and safer alternative for the management of inflammatory bowel disorders. [ABSTRACT FROM AUTHOR]

Background: Staphylococcus aureus (S. aureus) is one of the most important pathogens in burn infections colonized in the nose and increase the risk of infections. Methods: Overall, 85 S. aureus isolates were isolated from clinical and nasal hospitalized patients and health care workers (HCWs) in a burn unit and non-burn units in Isfahan from June 2016 and September 2016. Genes encoding penicillin-binding protein 2a (mecA) and adhesive surface proteins, including fibronectin-binding proteins (fnbA, fnbB), fibrinogen binding protein (fib), laminin-binding protein(eno), collagen binding protein (cna), elastin binding protein (ebps), intracellular adhesion operon (icaA and icaD) were detected using PCR method. Results: The rate of methicillin-resistant S. aureus (MRSA) among burn and non-burn isolates were 62% (18/29) and 25% (14/56), respectively. The most prevalent MSCRAMMs genes in burn units were eno (86%) and fib (66%). The most common gene pattern in burn center was icaA+fib+eno. The frequency of icaD, fib and ebpS was higher in clinical samples than nasal samples. No relation was found between the MSCRAMMs genes in the burn unit and non-burn units. Conclusion: The high prevalence of MRSA in burn center can be a new challenge for clinicians. The higher frequency of icaD, fib and ebpS in clinical isolates than nasal isolates may reflect the important role of these genes in colonization and pathogenesis of S. aureus.

Our previous work showed that using Lactobacillus pentosus HC-2 as a probiotic could improve the growth performance, immune response, gut bacterial diversity and disease resistance of L itopenaeus vannamei. However, the probiotic mechanism had not been fully characterized. In the present study, histology and proteomic analysis were performed to explore the influence of HC-2 surface protein on its probiotic effects on L. vannamei after feeding either the intact surface proteins, the probiotic treated with lithium chloride (LiCl) to remove noncovalently bound surface proteins or no probiotic for four weeks. Histological observation found that feeding with normal HC-2 obviously improved the intestinal histology and enhanced the protective effect against pathogen damage, but feeding with LiCl-treated HC-2 did not improve the intestinal environment. A total of over 2764 peptides and 1118 uniproteins were identified from the L. vannamei midgut; 211 proteins were significantly differentially expressed in the normal HC-2 group compared with the control group; 510 proteins were significantly differentially expressed in the LiCl-treated HC-2 group compared with the control group, and 458 proteins were significantly differentially expressed in the LiCl-treated HC-2 group compared with the normal HC-2 group. GO/KEGG enrichment analysis of the significantly different proteins demonstrated that feeding normal HC-2 mainly induced immune response, metabolic, cell adhesion and cell-cell signaling-related protein upregulation, which contributed to bacterial adhesion and colonization in the midgut to improve the shrimp immune system and growth, but these proteins were suppressed after the shrimp were fed bacteria deprived of surface proteins. Taken together, these results indicate that the surface proteins were indispensable for HC-2 to execute probiotic effects in the shrimp midgut. • Surface protein contributes to the improvement of intestinal histology of shrimp by L. pentosus HC-2. • The surface proteins of L. pentosus HC-2 did significantly influence the protein transcription in the shrimp midgut. • Probiotics mainly induce immune, metabolic, cell adhesion and cell-cell signaling proteins expression in the shrimp midgut. • Surface proteins were indispensable for HC-2 execute probiotic effects in midgut of shrimp. [ABSTRACT FROM AUTHOR]

The microbial surface components recognizing adhesive matrix molecules (MSCRAMMs) are a family of proteins that are defined by the presence of two adjacent IgG-like folded subdomains. These promote binding to ligands by mechanisms that involve major conformational changes exemplified by the binding to fibrinogen by the 'dock-lock-latch' mechanism or to collagen by the 'collagen hug'. Clumping factors A and B are two such MSCRAMMs that have several important roles in the pathogenesis of Staphylococcus aureus infections. MSCRAMM architecture, ligand binding, and roles in infection and colonization are examined with a focus on recent developments with clumping factors. Shear stress mechanical forces trigger interactions between MSCRAMMs and their ligands. MSCRAMMs bound to ligands via the dock-lock-latch or collagen-hug mechanisms can only be separated by very strong forces. Clumping factor A has a crucial role in attachment to the endothelium during endovascular infections. Clumping factor B binding to loricrin is important in early abscess formation as well as in adhesion to corneocytes. MSCRAMMs also bind a plethora of ligands by mechanisms that do not involve dock-lock-latch. [ABSTRACT FROM AUTHOR]

Others describe protein families spanning different species/genera including proteins related to the biofilm associated protein BAP of I S. aureus i (Valle et al.), polymer adhesion domain containing proteins (Järvå et al.) and collagen binding proteins (Arora et al.). Keywords: surface proteins; adhesion; biofilm; immune evasion; iron acquisition; pili; S-layer EN surface proteins adhesion biofilm immune evasion iron acquisition pili S-layer 1 3 3 05/25/21 20210521 NES 210521 The surfaces of Gram-positive bacterial cells are decorated with a diverse array of proteins including a large group that are covalently anchored to peptidoglycan by sortases. Surface proteins, adhesion, biofilm, immune evasion, iron acquisition, pili, S-layer. [Extracted from the article]

Our previous work showed that Lactobacillus pentosus HC-2 has high antibacterial and adhesion activity, and as a probiotic could improve the nutrients and immunomodulatory effects in the Litopenaeus vannamei farming. In order to further investigate the influence of HC-2 surface protein on its probiotic effects, the immune and digestion related genes expression and enzymes activities, the colonization numbers of HC-2, and the histologic characteristics were analysis in shrimp hepatopancreas after feeding either the intact surface proteins, the probiotic treated with lithium chloride (LiCl) to remove noncovalently bound surface proteins or no probiotic for four weeks. The results showed that the immune genes expression of lysozyme, proPO, LGBP, Penaeidins-3α, crustin and C-type lectin, the immune enzymes activities of superoxide dismutase, catalase and Alkaline phosphatase, and the digestion enzymes of Trypsin, Lipase and α-Amylase were significantly higher in hepatopancreas of shrimp fed with intact HC-2 than that in shrimp fed with base diet or striped surface proteins HC-2 post feeding and challenge. In addition, the shrimp fed with intact HC-2 leads to the bacteria cells adhesion to hepatopancreas was significantly higher than that in shrimp fed with no surface proteins HC-2. Furthermore, the tissue damages of hepatopancreas caused by pathogenic vibrio were obviously observed in shrimp fed with base diet or no surface proteins HC-2, but no signs of damages were found in shrimp fed with intact HC-2. These results demonstrate that surface proteins are important components for HC-2 to execute probiotic effect that improve hepatopancreas immune response and nutrition digestion to protect shrimp against pathogen damage. • Intact L. pentosus HC-2 could protect the shrimp hepatopancreas against pathogen damage. • Surface proteins contribute to L. pentosus HC-2 improving shrimp hepatopancreas immune response. • Surface proteins play a vital role in L. pentosus HC-2 adhesion and colonization in hepatopancreas. [ABSTRACT FROM AUTHOR]

Living organisms produce various membrane-enveloped organic and inorganic particles in the nanometer length scale. Among these particles, exosomes (a bilayer vesicle, extracellular organelle), poly-hydroxyalkanoates (monolayer, intracellular hydroxy-fatty acid granules), and magnetosomes (bilayer, intracellular iron particles) have been widely studied. In order to drive these particles toward biotechnological applications, surface engineering is crucial. Proteins exposed on the surfaces of these particles allow molecular engineers to display potent proteins or peptides of interest on the particles for specific functions. Upon surface protein presentation, such engineered particles can participate in diverse applications from protein purification to target clinical trials. This review article presents a summary of progress in the surface engineering of naturally produced particles in recent years. The concept underlying this surface engineering as well as the fundamentals of the synthesis and recovery of surface-engineered particles are also addressed in this review. The review concludes by highlighting surface engineering aspects that will facilitate further development of these nanoparticles for more applications. [ABSTRACT FROM AUTHOR]

Gram-positive bacteria of the genus Listeria contain many surface proteins covalently bound to the peptidogly-can. In the pathogenic species Listeria monocytogenes, some of these surface proteins mediate adhesion and entry into host cells. Specialized enzymes called sortases anchor these proteins to the cell wall by a mechanism involving processing and covalent linkage to the peptidoglycan. How bacteria coordinate the production of sortases and their respective protein substrates is currently unknown. The present work investigated whether the functional status of the sortase influences the level at which its cognate substrates are produced. The relative amounts of surface proteins containing an LPXTG sorting motif recognized by sortase A (StrA) were determined in isogenic wild-type and ΔsrtA strains of L. monocytogenes. The possibility of regulation at the transcriptional level was also examined. The results showed that the absence of SrtA did not affect the expression of any of the genes encoding LPXTG proteins. However, marked differences were found at the protein level for some substrates depending on the presence/absence of SrtA. In addition to the known "mis-sorting" of some LPXTG proteins caused by the absence of SrtA, the total amount of certain LPXTG protein species was lower in the AsrtA mutant. These data suggested that the rate of synthesis and/or the stability of a subset of LPXTG proteins could be regulated post-transcription-ally depending on the functionality of SrtA. For some LPXTG proteins, the absence of SrtA resulted in only a partial loss of the protein that remained bound to the peptidoglycan, thus providing support for additional modes of cell-wall association in some members of the LPXTG surface protein family. [ABSTRACT FROM AUTHOR]

Cwp19 is a putatively surface-located protein from Clostridium difficile. A recombinant N-terminal protein (residues 27-401) lacking the signal peptide and the C-terminal cell-wall-binding repeats (PFam04122) was crystallized using the sitting-drop vapour-diffusion method and diffracted to 2 Å resolution. The crystal appeared to belong to the primitive monoclinic space group P21, with unit-cell parameters a = 109.1, b = 61.2, c = 109.2 Å, β = 111.85°, and is estimated to contain two molecules of Cwp19 per asymmetric unit. [ABSTRACT FROM AUTHOR]

Staphylococcus aureus infections are associated with abscess formation and bacterial persistence; however, the genes that enable this lifestyle are not known. We show here that following intravenous infection of mice, S. aureus disseminates rapidly into organ tissues and elicits abscess lesions that develop over weeks but cannot be cleared by the host. Staphylococci grow as communities at the center of abscess lesions and are enclosed by pseudocapsules, separating the pathogen from immune cells. By testing insertional variants in genes for cell wall-anchored surface proteins, we are able to infer the stage at which these molecules function. Fibrinogen-binding proteins ClfA and ClfB are required during the early phase of staphylococcal dissemination. The heme scavenging factors IsdA and IsdB, as well as SdrD and protein A, are necessary for abscess formation. Envelope-associated proteins, Emp and Eap, are either required for abscess formation or contribute to persistence. Fluorescence microscopy revealed Eap deposition within the pseudocapsule, whereas Emp was localized within staphylococcal abscess communities. Antibodies directed against envelope-associated proteins generated vaccine protection against staphylococcal abscess formation. Thus, staphylococci employ envelope proteins at discrete stages of a developmental program that enables abscess formation and bacterial persistence in host tissues. [ABSTRACT FROM AUTHOR]

In the present study, we used a proteomic approach to identify surface-associated proteins from the probiotic bacterium Lactobacillus plantarum 299v. Proteins were extracted from the cell surface using a mild wash in phosphate buffer and analysed by sodium dodecyl sulphate-polyacrylamide gel electrophoresis. Gel bands were excised and in-gel digested with trypsin. The resulting peptides were analysed by capillary-LC-ESI-MS/MS. The peptide sequences were used for a database search and allowed identification of a total of 29 proteins, many of which could potentially be involved in the action of probiotics in the gastrointestinal tract. The results provide the basis for future studies on the molecular mechanisms of probiotics. [ABSTRACT FROM AUTHOR]

The group of exported proteins of a bacterium are those proteins that are sorted from the cytoplasm to the bacterial surface or to the surroundings of the microorganism. In probiotic bacteria, these proteins are of special relevance because they might determine important traits such as adhesion to intestinal surfaces and molecular cross-talking with the host. Current knowledge about the presence and biological relevance of exported proteins produced by the main genera of probiotic bacteria in the gastrointestinal environment is reviewed in this minireview. As will be seen, some of these proteins are involved in host adhesion or are able to modify certain signalization pathways within host cells, whereas others are important for the physiology of probiotic bacteria in the gastrointestinal tract. [ABSTRACT FROM AUTHOR]

Streptococcus suis is an important swine pathogen responsible for a diverse group of diseases. Studies on vaccines have focused on S. suis serotype 2 strains, which are the most invasive isolates worldwide. However, in China S. suis serotype 9 (SS9) is also a prevalent serotype, which is frequently isolated from diseased pigs. Little is known about immunogenic proteins for SS9. Therefore, an immunoproteomic-based approach was developed to identify immunogenic proteins of SS9. Cell wall proteins extracted from SS9 strain GZ0565 isolated from a diseased pig with meningitis were screened by two-dimensional Western blotting using anti-SS9 sera pooled from specific pathogen-free mice. Protein spots were excised from preparative gels and identified by matrix-assisted laser desorption ionization time-of-flight MS (MALDI-TOF-MS) or MALDI-TOF-TOF-MS, which led to the identification of eight immunogenic proteins (arginine deiminase, extracellular solute-binding protein, translation elongation factor Ts, neprilysin, peptide ATP-binding cassette transporter peptide-binding protein, pyruvate kinase, phosphate acetyltransferase, and fructose-bisphosphate aldolase). These immunogenic proteins, which are encoded by genes that are reasonably conserved among SS9 strains, could be developed as vaccine candidates. [ABSTRACT FROM AUTHOR]

Bacterial surface proteins are key players in host–symbiont or host–pathogen interactions. How these proteins are targeted and displayed at the cell surface are challenging issues of both fundamental and clinical relevance. While surface proteins of Gram-negative bacteria are assembled in the outer membrane, Gram-positive bacteria predominantly utilize their thick cell wall as a platform to anchor their surface proteins. This surface display involves both covalent and noncovalent interactions with either the peptidoglycan or secondary wall polymers such as teichoic acid or lipoteichoic acid. This review focuses on the role of enzymes that covalently link surface proteins to the peptidoglycan, the well-known sortases in Gram-positive bacteria, and the recently characterizedl,d-transpeptidases in Gram-negative bacteria. [ABSTRACT FROM AUTHOR]

Abstract: Although exopolysaccharides are important and often essential compounds of the biofilm matrix, recent evidences suggest that a group of surface proteins plays a leading role during the development of the microbial communities. The first member of this group of proteins was described in a Staphylococcus aureus bovine mastitis isolate and was named Bap, for biofilm-associated protein. Later on, other surface proteins homologous to Bap and involved in biofilm development have been described in many gram-positive and gram-negative bacteria. In this review, we have summarized our knowledge about three members of this group of proteins: Bap of S. aureus, Esp of Enterococcus faecalis and BapA of Salmonella enterica ser. Enteritidis. To cite this article: C. Latasa et al., C. R. Biologies 329 (2006). [Copyright &y& Elsevier]

Aims: To analyse the cellular mechanisms that influence Listeria monocytogenes adhesion onto inert surfaces under acidic growth conditions. Methods and Results: The adhesion capability of all the strains was significantly reduced after cultivation at constant pH 5 than at constant pH 7 and the cell surface was significantly less hydrophobic at pH 5 than at 7. At pH 5, the analyses of surface protein composition revealed that the flagellin was downregulated for all strains, which was confirmed by the absence of flagella and the P60 protein was upregulated for L. monocytogenes EGD-e, X-Li-mo 500 and 111. The use of L. monocytogenes EGD mutants revealed that flagellin could be involved in the adhesion process, but not P60 protein. It was also observed that the hydrophobic character was not linked to the presence or the absence of flagellin or P60 protein at the cell surface of L. monocytogenes. Conclusions: The decrease of L. monocytogenes adhesion at pH 5 could be attributed to the downregulation of the flagellin synthesis under the acidic conditions. Significance and Impact of the Study: Conservation of food product at pH 5 will delay bacterial adhesion and biofilm formation during food processing on inert surfaces when the product is contaminated with L. monocytogenes. [ABSTRACT FROM AUTHOR]

Abstract: A group of surface proteins sharing several structural and functional features is emerging as an important element in the biofilm formation process of diverse bacterial species. The first member of this group of proteins was identified in a Staphylococcus aureus mastitis isolate and was named Bap (biofilm-associated protein). As common structural features, Bap-related proteins: (i) are present on the bacterial surface; (ii) show a high molecular weight; (iii) contain a core domain of tandem repeats; (iv) confer upon bacteria the capacity to form a biofilm; (v) play a relevant role in bacterial infectious processes; and (vi) can occasionally be contained in mobile elements. This review summarizes recent studies that have identified and assigned roles to Bap-related proteins in biofilm biology and virulence. [Copyright &y& Elsevier]

Glycoproteins on the body surface of females of the rotifer Brachionus plicatilis are a key signal in their mate recognition system. When B. plicatilis Russian strain females were exposed to 50 mM EDTA or EGTA, several surface glycoproteins were removed. Females exposed to EDTA died, but remained intact and were used in mating bioassays with conspecifics males. Live control females elicited a male mating response in 21% of encounters, freeze-killed control females elicited responses in 23%, but EDTA extracted females elicited a mating response in only 5% of encounters. At least some of the EDTA-extractable proteins on the surface of females appear to be critical to male mate recognition. EDTA treated females could be exposed to proteins extracted from other females and some proteins re-attached to their body surface, restoring their attractiveness to males. SDS-PAGE of these proteins revealed 15–17 prominent bands, most ranging in molecular mass from 66 to 12 kD. The EDTA-extractable proteins were separated using ion exchange chromatography and each fraction was tested for its ability to restore female attractiveness. When proteins in fraction 22 were bound to females, they restored 80% of the females’ ability to elicit male mating responses. Exposing EDTA treated females to bovine serum albumin or casein had no effect on their attractiveness to males. EDTA treated females from different Brachionus clades and species were exposed to proteins from fraction 22. Female attractiveness could be restored in most clades of B. plicatilis, but no transfer of mating attractiveness was observed to B. rotundiformis or B. ibericus females. Conspecific males treated with EDTA and exposed to proteins in fraction 22 could not be feminized and made attractive to other males. A sexual dimorphism in surface proteins therefore exists between B. plicatilis females and males. Successful transfer of glycoproteins critical in mate recognition is dependent on signal glycoprotein structure and the structure of the other proteins present on the surface of females. [ABSTRACT FROM AUTHOR]

Infections caused by the Gram-positive bacterium Streptococcus pneumoniae have become a major health problem worldwide because of their high morbidity and mortality rates, especially in developing countries. This microorganism colonizes the human upper respiratory tract and becomes pathogenic under certain circumstances, which are not well known. In the interaction with the host, bacterial surface structures and proteins play major roles. To gain knowledge into gradual changes and adaptive mechanisms that this pathogen undergoes from when it enters the host, we mimicked several in vivo situations representing interaction with epithelial and macrophage cells, as well as a condition of presence in blood. Then, we analyzed, in four pneumococcal strains, two major surface structures, the capsule and extracellular vesicles produced by the pneumococci, as well as surface proteins by proteomics, using the "shaving" approach, followed by LC-MS/MS. We found important differences in both surface ultrastructures and proteins among the culture conditions and strains used. Thus, this work provides insights into physiological adaptations of the pneumococcus when it interacts with the host, which may be useful for the design of strategies to combat infections caused by this pathogen. [ABSTRACT FROM AUTHOR]

There is no effective vaccine against Streptococcus uberis mastitis in dairy cows. Objectives of this study were (1) to extract S. uberis surface proteins (SUSP) and determine immunoreactivity in vitro and (2) immunogenicity and efficacy in vivo. SUSP was extracted from S. uberis, and their immunoreactivity was tested by western blot. In total, 26 Jersey dairy cows were randomly divided into four groups. Groups 1, 2, and 3 were vaccinated subcutaneously with 4 mg, 1 mg, and 100 μg of SUSP, respectively, with Freund's incomplete adjuvant. Group 4 (control) was injected with placebo. S. uberis UT888 was infused into two contralateral quarters of each cow during early lactation. Somatic cell count (SCC), bacteria count in milk, and mastitis were monitored. Our results show that SUSP contains multiple protein bands, that ranged from 10 to 100 kDa. All vaccinates showed an increased anti-SUSP IgG antibody. The SCC of all experimentally infected quarters increased after challenge but slightly decreased after day 3 with no significant difference among groups. Milk bacterial count was significantly (p < 0.05) reduced in high and medium doses vaccinated groups than low and control groups. In conclusion, SUSP vaccine is immunogenic and showed a promising efficacy to control bovine S. uberis mastitis. [ABSTRACT FROM AUTHOR]

Incubation of eosinophils with schistosomula of Schistosoma mansoni in vitro induces changes in the eosinophil membrane. Cell surface proteins were blocked with unlabelled iodide and then, after incubation with schistosomula. newly accessible proteins were detected by lactoperoxidase catalysed iodination with radioactive iodide. Normal turnover restores several proteins to the eosinophil surface, but the schistosomula .specifically induced the appearance of a protein of mol. wt 18K. This protein has previously been detected when eosinophits interact with antibody coated agar layers. Soluble factors released by schistosomula induced the appearance of enhanced levels of 16 and 18K proteins. It has previously been shown that proteins involved in binding of eosinophils to IgG coated antigen coupled cellulose have mol. wts of 16K and 18K. [ABSTRACT FROM AUTHOR]

Certain methicillin-resistant Staphylococcus aureus strains contain a 230-kDa cell-wall protein which is not present on the surface of other staphylococci. The presence of this 230-kDa protein is associated with a negative test result in commercial assays designed to detect fibrinogen-binding proteins and/or protein A on the staphylococcal surface. We have purified and partially characterised the 230-kDa protein from a lysostaphin digest of a non-agglutinating methicillin-resistant S. aureus strain. Partial amino acid sequence data obtained from the purified protein did not reveal my significant similarities to known proteins which indicates that the protein is novel. The 230-kDa protein was very sensitive to proteolysis; soluble plasmin, or plasmin formed on the bacterial -cell surface, rapidly degraded the 230-kDa protein to a 175-kDa form. The finding that the 230-kDa protein bound to lectins allowed its purification by affinity chromatography on immobilised wheat germ agglutinin. Furthermore, the degradation of the 230-kDa protein was associated with an increased adherence of non-agglutinating methicillin-resistant S. aureus cells to solid-phase fibronectin, fibrinogen or IgG. [ABSTRACT FROM AUTHOR]

The effect of starch surface proteins on retrogradation of wheat starches were evaluated by rheometer, RVA, XRD, DSC, and TPA. An increase of the storage modulus and setback viscosity of starch pastes was observed after SDS and NaOH treatments. XRD resulted exhibited that recrystallinity of NaOH-treated and SDS-treated starch gels was increased to 10.33% and 11.15%, respectively, higher than that of native starch gel. Retrogradation enthalpy was increased from 3.5 J/g to 5.3 J/g for SDS-treated starch gels after 14 days storage at 4 °C. This was in line with the pronounced changes in gel firmness which was increased to 357g for SDS-treated starch. It suggested that removal of starch surface proteins apparently influenced the water mobility in starch gels and accelerated the retrogradation process. Image 1 • NaOH and SDS treatments were used to remove the starch surface proteins. • Removing proteins increased the storage modulus and setback viscosity of starch paste. • Recrystallinity of NaOH-treated and SDS-treated starch gels was higher than native one. • SDS treatment promoted retrogradation enthalpy from 3.5 J/g to 5.3 J/g. • Firmness increased from 261g for native starch to 357g for SDS-treated starch after storage. [ABSTRACT FROM AUTHOR]

Trueperella pyogenes is an opportunistic pathogen, responsible for important infections in pigs and significant economic losses in swine production. To date, there are no available commercial vaccines to control diseases caused by this bacterium. In this work, we performed a comparative proteomic analysis of 15 T. pyogenes clinical isolates, by "shaving" live cells, followed by LC-MS/MS, aiming at the identification of the whole set of surface proteins (i.e., the "pan-surfome") as a source of antigens to be tested in further studies as putative vaccine candidates, or used in diagnostic tools. A total of 140 surface proteins were detected, comprising 25 cell wall proteins, 10 secreted proteins, 23 lipoproteins and 82 membrane proteins. After describing the "pan-surfome", the identified proteins were ranked in three different groups based on the following criteria: to be (i) surface-exposed, (ii) highly conserved and (iii) widely distributed among different isolates. Two cell wall proteins, three lipoproteins, four secreted and seven membrane proteins were identified in more than 70% of the studied strains, were highly expressed and highly conserved. These proteins are potential candidates, alone or in combination, to obtain effective vaccines against T. pyogenes or to be used in the diagnosis of this pathogen. [ABSTRACT FROM AUTHOR]