TCS and SI carried out the antigen identification by mass-spectrometry. CK and SK performed Compound C the deep sequencing analysis of the HCDR3. CSH and ARMB conceived the study, and participated in its design and coordination and helped to draft the manuscript. All authors read and approved the final manuscript.”
“Background Vibrio anguillarum, a highly motile

marine member of the γ-Proteobacteria, is one of the causative agents of vibriosis, a fatal hemorrhagic septicemic disease of both wild and cultured fish, crustaceans, and bivalves [1]. Fish infected with V. anguillarum display skin discoloration and erythema around the mouth, fins, and vent. Necrotic lesions are also observed in the abdominal muscle [2]. Mortality rates in infected fish populations range as high as 30-100% [1, 3]. Vibriosis has caused severe economic losses to aquaculture worldwide [1, 3] and affects many farm-raised fish including Pacific salmon, Atlantic salmon, sea bass, cod, and eel [3, 4]. V. anguillarum enters its fish host through the gastrointestinal tract (GI) and quickly colonizes this nutrient rich environment [2, 5]. Garcia et al. [6] have www.selleckchem.com/small-molecule-compound-libraries.html shown that V. anguillarum grows extremely well in salmon intestinal

mucus and that mucus-grown cells specifically express a number of different proteins, including several outer membrane proteins [6] and the extracellular metalloprotease EmpA [2, 5]. Several genes have been reported to be correlated with virulence by V. anguillarum, including the vah1 hemolysin cluster [7, 8], the rtx hemolysin cluster [9], the siderophore mediated iron transport system [10], the empA metalloprotease [2, 5], and the flaA gene [11]. Hemolytic activity of V. anguillarum has been considered

to be the virulence factor responsible for hemorrhagic septicemia during infection [10]. We have identified two hemolysin gene clusters in V. anguillarum that contribute to the virulence of this pathogen [8, 9]. One gene cluster, rtxACHBDE, encodes a MARTX toxin and its type I secretion system [9]. The second hemolysin gene cluster in V. anguillarum strain M93Sm contains the hemolysin gene Montelukast Sodium vah1 flanked by two putative lipase-related genes (llpA and llpB) immediately downstream and upstream by a divergently transcribed hemolysin-like gene (plp) that appears to function as a repressor of vah1-dependent hemolytic activity [8]. The plp-encoded protein has very high sequence similarity to phospholipases found in other pathogenic Vibrio species [8]. However, the enzymatic characteristics of Plp in V. anguillarum were not described. Generally, phospholipases are divided into several subgroups depending on their specificity for hydrolysis of ester bonds at different locations in the phospholipid molecule.