Streptococcus thermophilus Cell Wall-Anchored Proteinase: Release, Purification, and Biochemical and Genetic Characterization

Fernandez-Espla, María Dolores; Garault, Peggy; Monnet, Véronique; Rul, Françoise

doi:10.1128/aem.66.11.4772-4778.2000

Cited by 143Enzyme Production and CharacterizationProbiotics and Fermented FoodsBacterial Genetics and Biotechnology

Streptococcus thermophilus Cell Wall-Anchored Proteinase: Release, Purification, and Biochemical and Genetic Characterization

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Fernandez-Espla, María Dolores, Garault, Peggy, Monnet, Véronique, Rul, Françoise·2000·Applied and Environmental Microbiology

DOI 10.1128/aem.66.11.4772-4778.2000PMC PMC92378

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Abstract

Streptococcus thermophilus CNRZ 385 expresses a cell envelope proteinase (PrtS), which is characterized in the present work, both at the biochemical and genetic levels. Since PrtS is resistant to most classical methods of extraction from the cell envelopes, we developed a three-step process based on loosening of the cell wall by cultivation of the cells in the presence of glycine (20 mM), mechanical disruption (with alumina powder), and enzymatic treatment (lysozyme). The pure enzyme is a serine proteinase highly activated by Ca(2+) ions. Its activity was optimal at 37 degrees C and pH 7.5 with acetyl-Ala-Ala-Pro-Phe-paranitroanilide as substrate. The study of the hydrolysis of the chromogenic and casein substrates indicated that PrtS presented an intermediate specificity between the most divergent types of cell envelope proteinases from lactococci, known as the PI and PIII types. This result was confirmed by the sequence determination of the regions involved in substrate specificity, which were a mix between those of PI and PIII types, and also had unique residues. Sequence analysis of the PrtS encoding gene revealed that PrtS is a member of the subtilase family. It is a multidomain protein which is maturated and tightly anchored to the cell wall via a mechanism involving an LPXTG motif. PrtS bears similarities to cell envelope proteinases from pyogenic streptococci (C5a peptidase and cell surface proteinase) and lactic acid bacteria (PrtP, PrtH, and PrtB). The highest homologies were found with streptococcal proteinases which lack, as PrtS, one domain (the B domain) present in cell envelope proteinases from all other lactic acid bacteria.

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Four different types of genes encoding CSPs of dairy lactic acid bacteria have been cloned and sequenced: prtB from L. bulgaricus, prtP from Lactococcus lactis and Lactobacillus casei, prtS from Streptococcus thermophilus, and prtH from Lactobacillus helveticus.
“So far, four different types of genes encoding CSPs of dairy lactic acid bacteria have been cloned and sequenced: prtB from L. bulgaricus, prtP from Lactococcus lactis and Lactobacillus casei, prtS from Streptococcus thermophilus, and prtH from Lactobacillus helveticus (8, 13, 18, 21, 28, 38).”
From Determination of the Domain of the Lactobacillus delbrueckii subsp. bulgaricus Cell Surface Proteinase PrtB Involved in Attachment to the Cell Wall after Heterologous Expression of the prtB Gene in Lactococcus lactis (2003) · cites this paper as [8]

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
Bradford, M. M. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90527-3 · Cited by 255,302 · see citing works
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961 · see citing works
Molecular Cloning: A Laboratory Manual
Sambrook, J., Fritsch, E., & Maniatis, T. (1989) · UCLA - Biblioteca de Ciencias de la Salud · Cited by 133,589 · see citing works
Short-Term Effects of Nose-Only Cigarette Smoke Exposure on Glutathione Redox Homeostasis, Cytochrome P450 1A1/2 and Respiratory Enzyme Activities in Mice Tissues
Raza, H., John, A., & Nemmar, A. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000350087 · Cited by 47,311 · see citing works
A comprehensive set of sequence analysis programs for the VAX
Devereux, J., Haeberli, P. E., & Smithies, O. (1984) · Nucleic Acids Research · doi:10.1093/nar/12.1part1.387 · Cited by 14,222 · see citing works
Cold Spring Harbor Laboratory; Cold Spring Harbor, NY
Cavalier-Smith, T. (1980) · FEBS Letters · doi:10.1016/0014-5793(80)80323-1 · Cited by 6,317 · see citing works
Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
Nielsen, H., Engelbrecht, J., Brunak, S., & von HEIJNE, G. (1997) · Protein Engineering Design and Selection · doi:10.1093/protein/10.1.1 · Cited by 5,324 · see citing works
On the size of the active site in proteases. I. Papain
Schechter, I., & Berger, A. (1967) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(67)80055-x · Cited by 5,203 · see citing works
Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels
Blum, H., Beier, H., & Gross, H. J. (1987) · Electrophoresis · doi:10.1002/elps.1150080203 · Cited by 4,150 · see citing works
Improved medium for lactic streptococci and their bacteriophages
Terzaghi, B. E., & Sandine, W. E. (1975) · Applied Microbiology · doi:10.1128/am.29.6.807-813.1975 · Cited by 2,339 · see citing works
Surface Proteins of Gram-Positive Bacteria and Mechanisms of Their Targeting to the Cell Wall Envelope
Navarre, W. W., & Schneewind, O. (1999) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.63.1.174-229.1999 · Cited by 1,391 · see citing works
Staphylococcus aureus Sortase, an Enzyme that Anchors Surface Proteins to the Cell Wall
Mazmanian, S. K., Liu, G., Ton-That, H., & Schneewind, O. (1999) · Science · doi:10.1126/science.285.5428.760 · Cited by 1,053 · see citing works
Subtilases: the superfamily of subtilisin-like serine proteases.
Siezen, R. J., & Leunissen, J. A. M. (1997) · Protein Science · doi:10.1002/pro.5560060301 · Cited by 896 · see citing works
A versatile quick-prep of genomic DNA from Gram-positive bacteria
Pospiech, A. (1995) · Trends in Genetics · doi:10.1016/s0168-9525(00)89052-6 · Cited by 744 · see citing works
The proteotytic systems of lactic acid bacteria
Kunji, E. R. S., Mierau, I., Hagting, A., Poolman, B., & Konings, W. N. (1996) · Antonie van Leeuwenhoek · doi:10.1007/bf00395933 · Cited by 715 · see citing works
Peptidases and amino acid catabolism in lactic acid bacteria
Christensen, J. E., Dudley, E. G., Pederson, J. A., & Steele, J. L. (1999) · Antonie van Leeuwenhoek · doi:10.1023/a:1002001919720 · Cited by 630 · see citing works
[4] Plasmid transformation of Escherichia coli and other bacteria
Hanahan, D., Jessee, J. A., & Bloom, F. R. (1991) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(91)04006-a · Cited by 621 · see citing works
Cell wall sorting signals in surface proteins of gram‐positive bacteria.
Schneewind, O., Mihaylova‐Petkov, D., & Model, P. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb06169.x · Cited by 426 · see citing works
Conservation of a hexapeptide sequence in the anchor region of surface proteins from Gram‐positive cocci
Fischetti, V. A., Pancholi, V., & Schneewind, O. (1990) · Molecular Microbiology · doi:10.1111/j.1365-2958.1990.tb02072.x · Cited by 411 · see citing works
Identification of an Antihypertensive Peptide from Casein Hydrolysate Produced by a Proteinase from Lactobacillus helveticus CP790
Maeno, M., Yamamoto, N., & Takano, T. (1996) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(96)76487-1 · Cited by 392 · see citing works
Genetics and Molecular Biology of Streptococci, Lactococci, and Enterococci
Dunny, G. M., Cleary, P. P., & McKay, L. L. (1991) · Cited by 353 · see citing works
Mode of Action of Glycine on the Biosynthesis of Peptidoglycan
Hammes, W. P., Schleifer, K. H., & Kandler, O. (1973) · Journal of Bacteriology · doi:10.1128/jb.116.2.1029-1053.1973 · Cited by 266 · see citing works
Nucleotide sequence of the cell wall proteinase gene of Streptococcus cremoris Wg2.
Kok, J., Leenhouts, K. J., Haandrikman, A. J., Ledeboer, A. M., & Venema, G. (1988) · Applied and Environmental Microbiology · doi:10.1128/aem.54.1.231-238.1988 · Cited by 199 · see citing works
Genetics of the proteolytic system of lactic acid bacteria
Kok, J. (1990) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1990.tb04877.x · Cited by 191 · see citing works
Primary Structure and Organization of the Gene for a Procaryotic, Cell Envelope-located Serine Proteinase
Vos, P., Simons, G., Siezen, R. J., & de Vos, W. M. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)80036-9 · Cited by 170 · see citing works
A maturation protein is essential for production of active forms of Lactococcus lactis SK11 serine proteinase located in or secreted from the cell envelope
Vos, P., van Asseldonk, M., van Jeveren, F., Siezen, R. J., Simons, G., & de Vos, W. M. (1989) · Journal of Bacteriology · doi:10.1128/jb.171.5.2795-2802.1989 · Cited by 167 · see citing works
Comparative Study of Action of Cell Wall Proteinases from Various Strains of Streptococcus cremoris on Bovine α s1 -, β-, and κ-Casein
Visser, S., Exterkate, F. A., Slangen, C. J., & de Veer, G. J. C. M. (1986) · Applied and Environmental Microbiology · doi:10.1128/aem.52.5.1162-1166.1986 · Cited by 160 · see citing works
Multi-domain, cell-envelope proteinases of lactic acid bacteria.
Siezen, R. J. (1999) · PubMed · Cited by 155 · see citing works
Complete nucleotide sequence of the streptococcal C5a peptidase gene of Streptococcus pyogenes.
Chen, C. C., & Cleary, P. P. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39748-0 · Cited by 155 · see citing works
Untitled work
(1981) · Cited by 154 · see citing works
Multi-domain, cell-envelope proteinases of lactic acid bacteria.
Siezen, R. J. (1999) · Antonie van Leeuwenhoek · doi:10.1023/a:1002036906922 · Cited by 144 · see citing works
Conservation of the C5a peptidase genes in group A and B streptococci
Chmouryguina, I. I., Suvorov, A. N., Ferrieri, P., & Cleary, P. P. (1996) · Infection and Immunity · doi:10.1128/iai.64.7.2387-2390.1996 · Cited by 132 · see citing works
Diversity of cell envelope proteinase specificity among strains of Lactococcus lactis and its relationship to charge characteristics of the substrate-binding region.
Exterkate, F. A., Alting, A. C., & Bruinenberg, P. G. (1993) · Applied and Environmental Microbiology · doi:10.1128/aem.59.11.3640-3647.1993 · Cited by 126 · see citing works
Selective amplification of cDNA sequence from total RNA by cassette-ligation mediated polymerase chain reaction (PCR): Application to sequencing 6·5 kb genome segment of hantavirus strain B-1
Isegawa, Y., Sheng, J., Sokawa, Y., Yamanishi, K., Nakagomi, O., & Ueda, S. (1992) · Molecular and Cellular Probes · doi:10.1016/0890-8508(92)90043-w · Cited by 123 · see citing works
A new cell surface proteinase: sequencing and analysis of the prtB gene from Lactobacillus delbruekii subsp. bulgaricus
Gilbert, C., Atlan, D., Blanc, B., Portailer, R., Germond, J. E., Lapierre, L., & Mollet, B. (1996) · Journal of Bacteriology · doi:10.1128/jb.178.11.3059-3065.1996 · Cited by 117 · see citing works
Associative Growth and Proteolysis of Streptococcus thermophilus and Lactobacillus bulgaricus in Skim Milk
Rajagopal, S. N., & Sandine, W. E. (1990) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(90)78745-0 · Cited by 114 · see citing works
Specific binding of the activator Mga to promoter sequences of the emm and scpA genes in the group A streptococcus
McIver, K. S., Heath, A., Green, B. D., et al. (1995) · Journal of Bacteriology · doi:10.1128/jb.177.22.6619-6624.1995 · Cited by 107 · see citing works
Cloning, sequencing and expression of the gene encoding the cell-envelope-associated proteinase from Lactobacillus paracasei subsp. paracasei NCDO 151
HOLCK, A., & NAeS, H. (1992) · Journal of General Microbiology · doi:10.1099/00221287-138-7-1353 · Cited by 106 · see citing works
Intracellular X‐prolyl dipeptidyl peptidase from Lactococcus lactis spp. lactis : purification and properties
Zevaco, C., Monnet, V., & Gripon, J. C. (1990) · Journal of Applied Bacteriology · doi:10.1111/j.1365-2672.1990.tb02886.x · Cited by 105 · see citing works
Self-citation
Peptide Accumulation and Bitterness in Cheddar Cheese Made Using Single-Strain Lactococcus lactis Starters with Distinct Proteinase Specificities
Broadbent, J. R., Strickland, M., Weimer, B. C., Johnson, M. E., & Steele, J. L. (1998) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(98)75581-x · Cited by 94 · see citing works
Genetic Characterization of a Cell Envelope-Associated Proteinase from Lactobacillus helveticus CNRZ32
Pederson, J. A., Mileski, G. J., Weimer, B. C., & Steele, J. L. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.15.4592-4597.1999 · Cited by 91 · see citing works
Purification and characterization of the mature, membrane-associated cell-envelope proteinase of Lactobacillus helveticus L89
Martín-Hernández, M. C., Alting, A. C., & Exterkate, F. A. (1994) · Applied Microbiology and Biotechnology · doi:10.1007/s002530050075 · Cited by 80 · see citing works
Engineering of the Lactococcus lactis serine proteinase by construction of hybrid enzymes
Vos, P., Boerrigter, I. J., Buist, G., Haandrikman, A. J., Nijhuis, M., de Reuver, M. B., Siezen, R. J., Venema, G., de Vos, W. M., & Kok, J. (1991) · "Protein Engineering, Design and Selection" · doi:10.1093/protein/4.4.479 · Cited by 77 · see citing works
Identification of compounds causing symbiotic growth ofStreptococcus thermophilusandLactobacillus bulgaricusin milk
Bautista, E. S., Dahiya, R. S., & Speck, M. L. (1966) · Journal of Dairy Research · doi:10.1017/s0022029900011985 · Cited by 76 · see citing works
L'état des connaissances en matière de nutrition des bactéries lactiques
Desmazeaud, M. (1983) · Le Lait · doi:10.1051/lait:1983629-63018 · Cited by 68 · see citing works
High cell wall-associated proteinase activity of some Streptococcus thermophilus strains (H-strains) correlated with a high acidification rate in milk
Shahbal, S., Hemme, D., & Desmazeaud, M. (1991) · Le Lait · doi:10.1051/lait:1991327 · Cited by 64 · see citing works
Specificity of two genetically related cell-envelope proteinases of Lactococcus lactis subsp. cremoris towards αs1-casein-(1–23)-fragment
Exterkate, F. A., Alting, A. C., & Slangen, C. J. (1991) · Biochemical Journal · doi:10.1042/bj2730135 · Cited by 58 · see citing works
The Conversion of the α-s1-Casein-(1-23)-Fragment by the Free and Bound Form of the Cell-Envelope Proteinase of Lactococcus lactis subsp. cremoris Under Conditions Prevailing in Cheese
Exterkate, F. A., & Alting, A. C. (1993) · Systematic and Applied Microbiology · doi:10.1016/s0723-2020(11)80242-0 · Cited by 57 · see citing works
Propriétés acidifiantes des bactéries lactiques thermophiles en relation avec la fabrication du yoghourt
Accolas, J.-P., Bloquel, R., Didienne, R., et al. (1977) · Le Lait · doi:10.1051/lait:1977561-5621 · Cited by 54 · see citing works
The lactococcal cell envelope proteinases: Differences, calcium-binding effects and role in cheese ripening
Exterkate, F. A. (1995) · International Dairy Journal · doi:10.1016/0958-6946(95)00042-9 · Cited by 52 · see citing works
Stability and Specificity of the Cell Wall-Associated Proteinase from Lactococcus lactis subsp. cremoris H2 Released by Treatment with Lysozyme in the Presence of Calcium Ions
Coolbear, T., Reid, J. R., & PRITCHARD, G. G. (1992) · Applied and Environmental Microbiology · doi:10.1128/aem.58.10.3263-3270.1992 · Cited by 41 · see citing works
Role of Calcium in Activity and Stability of the Lactococcus lactis Cell Envelope Proteinase
Exterkate, F. A., & Alting, A. C. (1999) · Applied and Environmental Microbiology · doi:10.1128/aem.65.4.1390-1396.1999 · Cited by 40 · see citing works
Engineering of the substrate-binding region of the sublilisin-like, cell-envelop proteinase of Lactococcus lactis
Siezen, R. J., Bruinenberg, P. G., Vos, P., Alen-Boerrigter, I. V., Nijhuis, M., Alting, A. C., Exterkate, F. A., & Vos, W. M. D. (1993) · "Protein Engineering, Design and Selection" · doi:10.1093/protein/6.8.927 · Cited by 40 · see citing works
Characterization of a Cell Envelope-Associated Proteinase Activity from Streptococcus thermophilus H-Strains
Shahbal, S., Hemme, D., & Renault, P. (1993) · Applied and Environmental Microbiology · doi:10.1128/aem.59.1.177-182.1993 · Cited by 36 · see citing works
The presence of two proteinases associated with the cell wall of Lactobacillus bulgaricus
Stefanitsi, D., Sakellaris, G., & Garel, J. (1995) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1995.tb07499.x · Cited by 35 · see citing works
Simple Tests for Predicting the Lytic Behavior and Proteolytic Activity of Lactococcal Strains in Cheese
Boutrou, R., Sepulchre, A., Gripon, J. C., & Monnet, V. (1998) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(98)70121-3 · Cited by 34 · see citing works
Self-citation
Amino acid requirements and peptidase activities of Streptococcus salivarius subsp. thermophilus
Neviani, E., Giraffa, G., Brizzi, A., et al. (1995) · Journal of Applied Bacteriology · doi:10.1111/j.1365-2672.1995.tb03141.x · Cited by 33 · see citing works
Purification and Characterization of the Cell Wall Proteinase of Lactobacillus casei Subsp. casei IFPL 731 Isolated from Raw Goat's Milk Cheese
de Palencia, P. F., Peláez, C., Romero, C., & Martín-Hernández, M. C. (1997) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf970125w · Cited by 30 · see citing works
Purification of the proteinase from group B streptococci that inactivates human C5a
Bohnsack, J. F., Zhou, X., Williams, P. A., et al. (1991) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(91)90129-n · Cited by 29 · see citing works
Partial characterization and comparison of cell wall proteinases from 5 strains of Streptococcus lactis
Monnet, V., Bars, D. L., Neviani, E., Neviani, E., & Gripon, J. C. (1987) · Le Lait · doi:10.1051/lait:198713 · Cited by 29 · see citing works
Self-citation
The diversity of potential cheese ripening characteristics of lactic acid starter bacteria: 1. Resistance to cell lysis and levels and cellular distribution of proteinase activities
Coolbear, T., Pillidge, C. J., & Crow, V. L. (1994) · International Dairy Journal · doi:10.1016/0958-6946(94)90003-5 · Cited by 25 · see citing works
14C-methylated β-casein as a substrate for plasmin, and its application to the study of milk protein transformations
Donnelly, W. J., Barry, J. G., & Richardson, T. (1980) · Biochimica et Biophysica Acta (BBA) - Protein Structure · doi:10.1016/0005-2795(80)90203-2 · Cited by 25 · see citing works
Role of C-Terminal Domains in Surface Attachment of the Fructosyltransferase of Streptococcus salivarius ATCC 25975
Rathsam, C., & Jacques, N. A. (1998) · Journal of Bacteriology · doi:10.1128/jb.180.23.6400-6403.1998 · Cited by 24 · see citing works
The Contribution of Caseins to the Amino Acid Supply for Lactococcus lactis Depends on the Type of Cell Envelope Proteinase
Flambard, B., Hélinck, S., Richard, J., & Juillard, V. (1998) · Applied and Environmental Microbiology · doi:10.1128/aem.64.6.1991-1996.1998 · Cited by 18 · see citing works
Interaction between proteolytic strains of Lactococcus lactis influenced by different types of proteinase during growth in milk
Flambard, B., Richard, J., & Juillard, V. (1997) · Applied and Environmental Microbiology · doi:10.1128/aem.63.6.2131-2135.1997 · Cited by 16 · see citing works
Prevention of C-terminal autoprocessing of Lactococcus lactis SK11 cell-envelope proteinase by engineering of an essential surface loop
Bruinenberg, P. M., de Vos, W. M., & Siezen, R. J. (1994) · Biochemical Journal · doi:10.1042/bj3020957 · Cited by 16 · see citing works
Release and partial characterization of cell-envelope proteinases fromLactococcus lactis subsp.lactis IFPL 359 andLactobacillus casei subsp. casei IFPL 731 isolated from raw goat,s-milk cheese
de Palencia, P. F., Pel�ez, C., Requena, T., & Mart�n-Hernandez, M. D. C. (1995) · European Food Research and Technology · doi:10.1007/bf01193207 · Cited by 12 · see citing works
Yoghurt. II. Growth stimulating factors for Streptococcus thermophilus.
Pette, J. W., & Lolkema, H. (1950) · Cited by 4 · see citing works

Flagged first, then by citations

Research works printed but not linked: 2

[29]29. Gibson, T. J. 1984. Studies on the Epstein Barr virus genome. Ph.D. thesis. University of Cambridge, Cambridge, England.
[58]58. Shankar, P. A., and F. L. Davies. 1978. Proteinase and peptidase activities of yogurt starter bacteria, p. 473. In Proceedings of the XX International Dairy Congress, Paris.

Sorted by citations

Proteolytic systems of lactic acid bacteria.
Savijoki, K., Ingmer, H., & Varmanen, P. (2006) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-006-0427-1 · Cited by 717 · see citing works
Lactobacillus helveticus: the proteolytic system
Griffiths, M. W., & Tellez, A. M. (2013) · Frontiers in Microbiology · doi:10.3389/fmicb.2013.00030 · Cited by 241 · see citing works
Variability of Hydrolysis of β-, αs1-, and αs2-Caseins by 10 Strains of Streptococcus thermophilus and Resulting Bioactive Peptides
Miclo, L., Roux, É., Genay, M., Brusseaux, É., Poirson, C., Jameh, N., Perrin, C., & Dary, A. (2012) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf202176d · Cited by 87 · see citing works
Simultaneous Presence of PrtH and PrtH2 Proteinases in Lactobacillus helveticus Strains Improves Breakdown of the Pure α s1 -Casein
Sadat-Mekmene, L., Jardin, J., Corre, C., Mollé, D., Richoux, R., Delage, M.-M., Lortal, S., & Gagnaire, V. (2011) · Applied and Environmental Microbiology · doi:10.1128/aem.01466-10 · Cited by 72 · see citing works
prtH2 , Not prtH , Is the Ubiquitous Cell Wall Proteinase Gene in Lactobacillus helveticus
Genay, M., Sadat, L., Gagnaire, V., & Lortal, S. (2009) · Applied and Environmental Microbiology · doi:10.1128/aem.02395-08 · Cited by 66 · see citing works
Allergenicity of acidic peptides from bovine β-lactoglobulin is reduced by hydrolysis with Bifidobacterium lactis NCC362 enzymes.
Prioult, G., Pecquet, S., & Fliss, I. (2005) · International Dairy Journal · doi:10.1016/j.idairyj.2004.09.001 · Cited by 44 · see citing works
Determination of the Domain of the Lactobacillus delbrueckii subsp. bulgaricus Cell Surface Proteinase PrtB Involved in Attachment to the Cell Wall after Heterologous Expression of the prtB Gene in Lactococcus lactis
Germond, J.-E., Delley, M., Gilbert, C., & Atlan, D. (2003) · Applied and Environmental Microbiology · doi:10.1128/aem.69.6.3377-3384.2003 · Cited by 36 · see citing works
Release of the cell envelope protease PrtS in the growth medium of Streptococcus thermophilus 4F44
Chang, O. K., Perrin, C., Galia, W., Saulnier, F., Miclo, L., Roux, E., Driou, A., Humbert, G., & Dary, A. (2012) · International Dairy Journal · doi:10.1016/j.idairyj.2011.10.014 · Cited by 31 · see citing works
Lactocepin: the cell envelope-associated Endopeptidase of lactococci.
Broadbent, J. R., & Steele, J. L. (2013) · Handbook of Proteolytic Enzymes · doi:10.1016/b978-0-12-382219-2.00703-1 · Cited by 6 · see citing works

Structure of the Bacterial Cell Wall.
Umeda, A., & Amako, K. (1998) · Nippon Ishinkin Gakkai Zasshi · doi:10.3314/jjmm.39.147 · Cited by 7 · see citing works
Activation of the Alternative Complement Pathway by Pneumococcal Cell Wall Teichoic Acid
Winkelstein, J. A., & Tomasz, A. (1978) · The Journal of Immunology · doi:10.4049/jimmunol.120.1.174 · Cited by 150 · see citing works
Molecular Arrangement of Teichoic Acid in the Cell Wall of Staphylococcus lactis
Archibald, A. R., BADDILEY, J., & Heckels, J. E. (1973) · Nature New Biology · doi:10.1038/newbio241029a0 · Cited by 31 · see citing works
Teichoic acids anchor distinct cell wall lamellae in an apically growing bacterium
Ultee, E., van der Aart, L. T., Zhang, L., van Dissel, D., Diebolder, C. A., van Wezel, G. P., Claessen, D., & Briegel, A. (2020) · Communications Biology · doi:10.1038/s42003-020-1038-6 · Cited by 33 · see citing works
Taking aim at wall teichoic acid synthesis: new biology and new leads for antibiotics
Sewell, E. W., & Brown, E. D. (2013) · The Journal of Antibiotics · doi:10.1038/ja.2013.100 · Cited by 128 · see citing works

Authors: Fernandez-Espla, M. D., Garault, P., Monnet, V., & Rul, F.
Affiliations: Unité de Recherche de Biochimie et Structure des Protéines, Institut National de la Recherche Agronomique, 78352 Jouy-en-Josas Cedex, France
Institut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement (FR)
ORCID: Garault, Peggy
Venue: Applied and Environmental Microbiology
Publisher: American Society for Microbiology
Published: 2000-11
Volume: 66
Issue: 11
Pages: 4772-4778
ISSN: 0099-2240 (ISSN-L)
1098-5336
DOI: 10.1128/aem.66.11.4772-4778.2000
PMC: PMC92378
OpenAlex: W2104046960
Cited by: 143
References: 68
Citations by year: 2026: 3 · 2025: 1 · 2024: 2 · 2023: 5 · 2022: 2 · 2021: 11 · 2020: 10 · 2019: 2 · 2018: 4 · 2017: 4 · 2016: 8 · 2015: 7 · 2014: 9 · 2013: 7 · 2012: 9
FWCI: 4.00
Type: journal article
Language: en
Open access: green
europepmc.org
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Applied and Environmental Microbiology (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
HAL (submittedVersion)
Funders: European Commission
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
Life Sciences › Agricultural and Biological Sciences › Food Science › Probiotics and Fermented Foods
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Keywords: Streptococcus thermophilus, cell envelope proteinase, PRT, serine protease, LPXTG motif, protease purification, substrate specificity, calcium activation, enzyme maturation, lactic acid bacteria, pyogenic streptococci
MeSH terms: Amino Acid Sequence, Bacterial Proteins, Calcium Chloride, Cell Wall, Enzyme Activation, Genes, Bacterial, Molecular Sequence Data, Serine Endopeptidases, Streptococcus, Substrate Specificity, Sequence Alignment, Sequence Homology, Amino Acid, Sequence Analysis, DNA, Protein Structure, Tertiary

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Streptococcus thermophilus Cell Wall-Anchored Proteinase: Release, Purification, and Biochemical and Genetic Characterization

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