Bovine Lactogenic Immunity Against Pediatric Enteropathogens

Boesman-Finkelstein, Mary; Finkelstein, Richard A.

doi:10.1007/978-1-4615-3838-7_46

Cited by 9 publications

(11 citation statements)

References 33 publications

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“…The HA/P of V. chokrue 01 is recognized as a virulence factor in pathogenesis of cholera [14]. It has been reported that HA/P contributes to pathogenesis by degrading several physiologically important substances of host 1193, including mucin, fibronectin and secretory IgA, and by activating the cholera enterotoxin (CT) with nicking A subunit of the toxin [20].…”

Section: Discussionmentioning

confidence: 99%

“…It has been reported that HA/P contributes to pathogenesis by degrading several physiologically important substances of host 1193, including mucin, fibronectin and secretory IgA, and by activating the cholera enterotoxin (CT) with nicking A subunit of the toxin [20]. Recently, Finkelstein et al [14] have reported HA/P works as detachase which facilitate detaching of the V. choterue organism from host epithelial cells. Present study gave a conclusive evidence that a new epidemic 0139 V. cholerue dose produce a protease indistinguishable from that of V. cholerae 01, suggesting that the protease is another virulence factor of V. cholerue 0139.…”

Section: Discussionmentioning

confidence: 99%

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Vibrio cholerae O139 produces a protease which is indistinguishable from the haemagglutinin/protease of Vibrio cholerae O1 and non-O1

Naka¹,

Yamamoto²,

Albert³

et al. 1995

FEMS Immunology and Medical Microbiology

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Haemaglutinin/protease (HA/P) is one of the virulence factors of Vibrio cholerae O1 and pathogenic strains of V. cholerae non-O1. In this study, we examined protease activity of a new serogroup of Vibrio cholerae recently designated as O139 synonym Bengal. The protease activity was produced by all eight isolates of V. cholerae O139 from Bangladeshi patients. Purification and partial characterization of the protease from V. cholerae O139 demonstrated the purified protease (O139-P) was indistinguishable from that previously reported for HA/P of V. cholerae non-O1 (NAG-HA/P) and V. cholerae O1 (Vc-HA/P). These results prove that V. cholerae O139 produces a protease belonging to HA/P, and suggest that the protease is another virulence factor found in newly emerged V. cholerae O139, as in V. cholerae O1.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Vibrio cholerae O139 produces a protease which is indistinguishable from the haemagglutinin/protease of Vibrio cholerae O1 and non-O1

Naka¹,

Yamamoto²,

Albert³

et al. 1995

FEMS Immunology and Medical Microbiology

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“…Simultaneously, the accumulation of quorum-sensing molecules induces the expression of the hap gene encoding the Hap protease. The role of this protease is suggested to be that of a 'detachase', allowing V. cholerae to be freed from the intestine walls in order to re-enter the environment [151].…”

Section: Autoinducer 2: a Universal Language?mentioning

confidence: 99%

Microbial quorum sensing: a tool or a target for antimicrobial therapy?

Raina

Vizio

Odell

et al. 2009

Biotech and App Biochem

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Inter-cell communication aided by released chemical signals when cell density reaches a critical concentration has been investigated for over 30 years as quorum sensing. Originally discovered in Gram-negative bacteria, quorum-sensing systems have also been studied extensively in Gram-positive bacteria and dimorphic fungi. Microbial communities communicating via quorum sensing employ various chemical signals to supervise their surrounding environment, alter genetic expression and gain advantage over their competitors. These signals vary from acylhomoserine lactones to small modified or unmodified peptides to complex gamma-butyrolactone molecules. The scope of this review is to give an insight into some of the quorum-sensing systems now known and to explore their role in microbial physiology and development of pathogenesis. Particular attention will be dedicated to the signalling molecules involved in quorum-sensing-mediated processes and the potential shown by some of their natural and synthetic analogues in the treatment of infections triggered by quorum sensing.

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“…Many investigators have postulated the possible roles of V. cholerue protease. At first, it was thought to be involved in bacterial colonization, because digestion of mucin and/or fibronectin might facilitate vibrio approximation to the eukaryotic cell surface [2]. Nevertheless, recent experiments using protaase-deficient mutants showed that they still had the ability to attach to cultured human intestinal epithelial cells [3] and the protease was likely to play a role io detachment more than in attachment [3].…”

Section: Introductionmentioning

confidence: 99%

“…Nevertheless, recent experiments using protaase-deficient mutants showed that they still had the ability to attach to cultured human intestinal epithelial cells [3] and the protease was likely to play a role io detachment more than in attachment [3]. V. cholarm protease was also considered to nick and activhte the A subunit of cholera toxin (CT) [2]. However, ;the wide distribution of the protease among non-CT-producing V. cholerue non-01 strains suggested more biological roles.…”

Section: Introductionmentioning

confidence: 99%

Effect of Vibrio cholerae non-O1 protease on lysozyme, lactoferrin and secretory immunoglobulin A

Toma¹

1996

FEMS Microbiology Letters

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The effect of Vibrio cholerae non-O1 protease on host defense proteins (lysozyme, secretory immunoglobulin A and lactoferrin) was studied in relation to its virulence mechanism. The proteins treated with the protease were analysed by SDS-PAGE. There was no influence of the protease on lysozyme. The protease cleaved lactoferrin into two fragments of 50 kDa and 34 kDa. N-terminal amino acid sequencing of these fragments revealed that the cleavage site was near the hinge region, between serine 420 and serine 421. This cleavage could affect the transition from open to closed configuration which is involved in iron binding and release. The anti-bacterial activity of lactoferrin was not affected by protease treatment. Secretory immunoglobulin A yielded a 42-kDa protein as the cleavage product. The susceptibility of secretory immunoglobulin A to V. cholerae non-O1 protease suggests a mechanism by which bacteria might evade the effect of this immunoglobulin.

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Bovine Lactogenic Immunity Against Pediatric Enteropathogens

Cited by 9 publications

References 33 publications

Vibrio cholerae O139 produces a protease which is indistinguishable from the haemagglutinin/protease of Vibrio cholerae O1 and non-O1

Vibrio cholerae O139 produces a protease which is indistinguishable from the haemagglutinin/protease of Vibrio cholerae O1 and non-O1

Microbial quorum sensing: a tool or a target for antimicrobial therapy?

Effect of Vibrio cholerae non-O1 protease on lysozyme, lactoferrin and secretory immunoglobulin A

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