Purification and Partial Characterization of a Prolyl-Dipeptidyl Aminopeptidase from
            <i>Lactobacillus helveticus</i>
            CNRZ 32

Khalid, Noraini M.; Marth, Elmer H.

doi:10.1128/aem.56.2.381-388.1990

Cited by 102 publications

(15 citation statements)

References 29 publications

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“…3B), as has also been demonstrated for some other metalloenzymes, e.g. a collagenase from Clostridium histolyticum [25], thermolysin [26], and a metallopeptidase from Lactobacillus helveticus [27]. The optimal LiCl salt concentration for PrtV proteolytic activity was 0.2 m, but the activity was enhanced in the presence of NaCl or KCl at concentrations of up to 0.5 m (Fig.…”

Section: Optimum Conditions For the Stability And Processing Of The Psupporting

confidence: 72%

The metalloprotease PrtV from Vibrio cholerae

et al. 2008

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Vibrio cholerae, the causative agent of cholera, is a Gram-negative motile bacterial species acquired via ingestion of contaminated food or water. Little is known regarding the environmental survival factors that exist in V. cholerae and play an important role in maximizing the ability of the vibrios to survive and multiply in the environment interacting with predators. In a recent study, we established that Caenorhabditis elegans is useful as a model system for identifying and assessing factors from V. cholerae other than cholera toxin that may contribute to pathogenesis and damage to host organisms [1]. Using reverse molecular genetics techniques, we identified an extracellular protease, the previously uncharacterized PrtV protein, as being necessary for killing of nematodes by V. cholerae [1]. The killing effect is associated with colonization of the C. elegans intestine. The elucidation of mechanisms behind this role for PrtV is of importance for the further understanding of V. cholerae environmental survival and bacteria-host interaction.Tissue barriers to pathogen invasion, such as extracellular matrices, epidermal keratinocyte layers and blood vessel walls, may be targeted by bacterial proteases. Proteolysis of host tissue components, such as extracellular matrix proteins, including collagen, laminin, fibronectin and elastin, could induce necrotic tissue damage [2,3]. Pseudomonas aeruginosa and Serratia mercescens proteases can degrade corneal proteoglycan ground substance and cause keratitis [4,5]. The blood clotting system plays a role in immobilization of invading pathogens and prevention of their dissemination. A pathogen can either use an arsenal of its own proteases, or induce the host fibrinolytic system(s) to dissolve the fibrin clot [6]. Yersinia pestis, the The Vibrio metalloprotease PrtV was purified from the culture supernatant of a Vibrio cholerae derivative that is deficient in several other secreted peptidases, including the otherwise abundant hemagglutinin ⁄ protease HapA. The PrtV is synthesized as a 102 kDa protein, but undergoes several N-and C-terminal processing steps during V. cholerae envelope translocation and prolonged incubation. Purified V. cholerae PrtV protease forms of 81 or 73 kDa were stabilized by calcium ions. Removal of calcium resulted in further rapid autoproteolysis. The two major products of autoproteolysis of the PrtV protease were approximately 37 and 18 kDa and could not be separated under non-denaturing conditions, indicating they are interacting domains. In an assay using cultured cells of the human intestinal cell line HCT8, the PrtV protein showed a cytotoxic effect leading to cell death. Using human blood plasma as a source of potential substrates of mammalian origin for the PrtV protease, we found that the extracellular matrix components fibronectin and fibrinogen were degraded by the enzyme. Additional tests with individual protein substrates revealed that plasminogen was also a possible target for the PrtV protease.OnlineOpen: This article is available fre...

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Section: Optimum Conditions For the Stability And Processing Of The Psupporting

confidence: 72%

The metalloprotease PrtV from Vibrio cholerae

et al. 2008

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“…The X-PD from Lb. helveticus is somewhat different in having a native monomeric size of 72 kDa [94].…”

Section: Proline-specific Peptidasesmentioning

confidence: 97%

“…The observation that most of the LEP I endopeptidase activity was present in the cell wall fraction was not substantiated [108]. Except for one report [91], all publications concerning X-prolyl dipeptidyl aminopeptidase agree on an intracellular location for this enzyme ( [90,92,93,94]; see below). The location of the prolidase from L. lactis ssp.…”

Section: Peptidase Localizationmentioning

confidence: 98%

“…Aminopeptidase P, proline iminopeptidase, iminodipeptidase (prolinase), imidodipeptidase (prc~ lidase) and X-prolyl dipeptidyl aminopeptidase (X-PDAP) have all been detected in the various species of lactic acid bacteria [70,75,78,[87][88][89][90][91][92][93][94][95]. Several of these enzymes have been purified to homogeneity and characterized in detail ( [88,[90][91][92]94,95]; see Table 3). All X-PDAPs specifically degrade peptides of the structure X-Pro-Y... (X and Y can be any amino acid) but the rate of hydrolysis depends on the type of amino acids surrounding proline.…”

Section: Proline-specific Peptidasesmentioning

confidence: 99%

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Genetics of the proteolytic system of lactic acid bacteria

Kok

1990

FEMS Microbiology Letters

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“…delbrueckii subsp, bulgaricus [167][168][169], Lb. helreticus [170], Lb. lactis and S. thermophilus [171].…”

Section: Peptidasesmentioning

confidence: 99%

The physiology and biochemistry of the proteolytic system in lactic acid bacteria

Pritchard

Coolbear²

1993

FEMS Microbiology Reviews

274

155

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The inability of lactic acid bacteria to synthesize many of the amino acids required for protein synthesis necessitates the active functioning of a proteolytic system in those environments where protein constitutes the main nitrogen source. Biochemical and genetic analysis of the pathway by which exogenous proteins supply essential amino acids for growth has been one of the most actively investigated aspects of the metabolism of lactic acid bacteria especially in those species which are of importance in the dairy industry, such as the lactococci. Much information has now been accumulated on individual components of the proteolytic pathway in lactococci, namely, the cell envelope proteinase(s), a range of peptidases and the amino acid and peptide transport systems of the cell membrane. Possible models of the proteolytic system in lactococci can be proposed but there are still many unresolved questions concerning the operation of the pathway in vivo. This review will examine current knowledge and outstanding problems regarding the proteolytic system in lactococci and also the extent to which the lactococcal system provides a model for understanding proteolysis in other groups of lactic acid bacteria.

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Purification and Partial Characterization of a Prolyl-Dipeptidyl Aminopeptidase from Lactobacillus helveticus CNRZ 32

Cited by 102 publications

References 29 publications

The metalloprotease PrtV from Vibrio cholerae

The metalloprotease PrtV from Vibrio cholerae

Genetics of the proteolytic system of lactic acid bacteria

The physiology and biochemistry of the proteolytic system in lactic acid bacteria

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