Abstract
The discovery of outer membrane proteins (OMPs) with desirable specificity and surface availability is a fundamental challenge to develop accurate immunodiagnostic assay and multivalent vaccine of pathogenic Vibrio species in food and aquaculture. Herein 101 OMPs were systemically screened from 4,831 non-redundant proteins of Vibrio parahaemolyticus by bioinformatical predication of signaling peptides, transmembrane (TM) α-helix, and subcellular location. The sequence homology analysis with 32 species of Vibrio spp. and all the non-Vibrio strains revealed that 15 OMPs were conserved in at least 23 Vibrio species, including BamA (VP2310), GspD (VP0133), Tolc (VP0425), OmpK (VP2362), OmpW (VPA0096), LptD (VP0339), Pal (VP1061), flagellar L-ring protein (VP0782), flagellar protein MotY (VP2111), hypothetical protein (VP1713), fimbrial assembly protein (VP2746), VacJ lipoprotein (VP2214), agglutination protein (VP1634), and lipoprotein (VP1267), Chitobiase (VP0755); high adhesion probability of flgH, LptD, OmpK, and OmpW indicated they were potential multivalent Vibrio vaccine candidates. V. parahaemolyticus OMPs were found to share high homology with at least one or two Vibrio species, 19 OMPs including OmpA like protein (VPA073), CsuD (VPA1504), and MtrC (VP1220) were found relatively specific to V. parahaemolyticus. The surface proteomic study by enzymatical shaving the cells showed the capsular polysaccharides most likely limited the protease action, while the glycosidases improved the availability of OMPs to trypsin. The OmpA (VPA1186, VPA0248, VP0764), Omp (VPA0166), OmpU (VP2467), BamA (VP2310), TolC (VP0425), GspD (VP0133), OmpK (VP2362), lpp (VPA1469), Pal (VP1061), agglutination protein (VP1634), and putative iron (III) compound receptor (VPA1435) have better availability on the cell surface.
Highlights
Vibrio spp. are halophilic bacteria that are widely distributed in seawater, offshore sediments, marine life, and seafood products (Hackbusch et al, 2020)
The surface proteome based on enzymatical shaving of the extracellular peptides of the cells and massive identification of the peptides provides an experimental insight of the surface available Outer membrane proteins (OMPs)
The two comprehensive and complementary strategies were both adopted in this work to study the diagnostic surface antigens of V. parahaemolyticus and Vibrio species
Summary
Vibrio spp. are halophilic bacteria that are widely distributed in seawater, offshore sediments, marine life, and seafood products (Hackbusch et al, 2020). The vibriosis caused by Vibrio species (e.g., V. parahaemolyticus, Vibrio anguillarum, Vibrio alginolyticus, Vibrio ordalii, and Vibrio harveyi) has been found to cause an infection in more than 50 economic fish species and is considered a major economic threat to the marine aquaculture industry (Yu et al, 2016). Polyvalent vaccines that cover the main serotypes of the pathogen are preferred when compared with the monovalent vaccine that contains a single strain of a single antigen (Schlingmann et al, 2018). The traditional strategy of Vibrio polyvalent vaccines is based on the whole-cell antigens of representative strains like V. alginolyticus, V. parahaemolyticus (Aly et al, 2020). Outer membrane proteins (OMPs) are currently the main candidate antigens used in polyvalent vaccine studies for their essential function, surface exposure, and conservation among different strains (Pore and Chakrabarti, 2013). There have been some studies of the OmpK and OmpU as polyvalent vaccine candidates (Duperthuy et al, 2010; Li et al, 2010b), while many studies focus on the discovery of more multivalent and potent Omps for future vaccine development
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