Cloning of the gene encoding streptococcal immunoglobulin A protease and its expression in Escherichia coli

Gilbert, Joanne V.; Plaut, Andrew G.; Fishman, Yolanta; Wright, Andrew

doi:10.1128/iai.56.8.1961-1966.1988

Cited by 27 publications

(21 citation statements)

References 33 publications

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“…58, 1990 on August 5, 2020 by guest http://iai.asm.org/ Downloaded from al. (11) recently demonstrated that a cloned IgAl protease gene from S. sanguis fails to hybridize with DNA from protease-producing S. pneumoniae. This may reflect the distant genetic relationship (20 to 30% DNA-DNA homology) previously observed between these two species (22).…”

Section: Discussionmentioning

confidence: 99%

Molecular aspects of immunoglobulin A1 degradation by oral streptococci

Reinholdt¹,

Tomana²,

Mortensen³

et al. 1990

Infect Immun

103

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Using a panel of 143 strains classified according to a novel taxonomic system for oral viridans-type streptococci, we reexamined the ability of oral streptococci to attack human immunoglobulin Al (IgAl) molecules with IgAl protease or glycosidases. IgAl protease production was an exclusive property of all strains belonging to Streptococcus sanguis and Streptococcus oralis (previously S. mitior) and of some strains of Streptococcus mitis biovar 1. These are all dominant initiators of dental plaque formation. Degradation of the carbohydrate moiety of IgAl molecules accompanied IgAl protease activity in S. oralis and protease-producing strains of S. mitis biovar 1. Neuraminidase and I8-galactosidase were identified as extracellular enzymes in organisms of these taxa. By examination with enzyme-neutralizing antisera, four distinct IgAl proteases were detected in S. sanguis biovars 1 to 3, S. sanguis biovar 4, S. oralis, and strains of S. mitis, respectively. The cleavage of IgAl molecules by streptococcal IgA proteases was found to be influenced by their state of glycosylation. Treatment of IgAl with bacterial (including streptococcal) neuraminidase increased susceptibility to protease, suggesting a cooperative activity of streptococcal IgAl protease and neuraminidase. In contrast, a decrease in susceptibility was observed after extensive deglycosylation of the hinge region with endo-cL-N acetylgalactosaminidase. The effector functions of IgA antibodies depend on the carbohydrate-containing Fc portion. Hence, the observation that oral streptococci may cleave not only the al chains but also the carbohydrate moiety of IgAl molecules suggests that the ability to evade secretory immune mechanisms may contribute to the successful establishment of these bacteria in the oral cavity. 1186 on August 5, 2020 by guest http://iai.asm.org/ Downloaded from

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Section: Discussionmentioning

confidence: 99%

Molecular aspects of immunoglobulin A1 degradation by oral streptococci

Reinholdt¹,

Tomana²,

Mortensen³

et al. 1990

Infect Immun

103

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“…Cloning of streptococcal IgA1 genes from Streptococcus sanguis ATCC 10556 (70) and S. pneumoniae (229,308) has been reported. Hybridization experiments with an S. sanguis IgA1 protease gene probe showed no detectable homology to chromosomal DNA of gram-negative bacteria secreting IgA1 proteases.…”

Section: E Coli (I) Membrane Proteasesmentioning

confidence: 99%

Molecular and Biotechnological Aspects of Microbial Proteases

Rao

Tanksale

Ghatge

et al. 1998

Microbiol Mol Biol Rev

1,764

721

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SUMMARY Proteases represent the class of enzymes which occupy a pivotal position with respect to their physiological roles as well as their commercial applications. They perform both degradative and synthetic functions. Since they are physiologically necessary for living organisms, proteases occur ubiquitously in a wide diversity of sources such as plants, animals, and microorganisms. Microbes are an attractive source of proteases owing to the limited space required for their cultivation and their ready susceptibility to genetic manipulation. Proteases are divided into exo- and endopeptidases based on their action at or away from the termini, respectively. They are also classified as serine proteases, aspartic proteases, cysteine proteases, and metalloproteases depending on the nature of the functional group at the active site. Proteases play a critical role in many physiological and pathophysiological processes. Based on their classification, four different types of catalytic mechanisms are operative. Proteases find extensive applications in the food and dairy industries. Alkaline proteases hold a great potential for application in the detergent and leather industries due to the increasing trend to develop environmentally friendly technologies. There is a renaissance of interest in using proteolytic enzymes as targets for developing therapeutic agents. Protease genes from several bacteria, fungi, and viruses have been cloned and sequenced with the prime aims of (i) overproduction of the enzyme by gene amplification, (ii) delineation of the role of the enzyme in pathogenecity, and (iii) alteration in enzyme properties to suit its commercial application. Protein engineering techniques have been exploited to obtain proteases which show unique specificity and/or enhanced stability at high temperature or pH or in the presence of detergents and to understand the structure-function relationships of the enzyme. Protein sequences of acidic, alkaline, and neutral proteases from diverse origins have been analyzed with the aim of studying their evolutionary relationships. Despite the extensive research on several aspects of proteases, there is a paucity of knowledge about the roles that govern the diverse specificity of these enzymes. Deciphering these secrets would enable us to exploit proteases for their applications in biotechnology.

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“…Cloning of the gene from serotype b shows that the enzyme also has strong homology with the proteinase from N. gonorrhoeae, both having precursors which undergo similar processing on secretion [102]. The gene for the IgA proteinase from the oral bacterium, Streptococcus sanguis, has also been cloned [103]. It does not hybridize with chromosomal DNA of gram-negative bacteria that excrete IgA proteinase or S. pneumoniae, although the IgA proteinases of these two streptococcal species cleave the identical peptide bond in the human IgAl heavy-chain hinge region.…”

Section: Bacterial Iga Proteinasesmentioning

confidence: 99%