{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,26]],"date-time":"2026-09-26T10:41:09Z","timestamp":1790419269274,"version":"4.1.0"},"reference-count":28,"publisher":"American Society for Microbiology","issue":"2","license":[{"start":{"date-parts":[[1998,2,1]],"date-time":"1998-02-01T00:00:00Z","timestamp":886291200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Infect Immun"],"published-print":{"date-parts":[[1998,2]]},"abstract":"<jats:title>ABSTRACT<\/jats:title><jats:p>A recent study with isogenic strains constructed by recombinant DNA strategies unambiguously documented that a highly conserved extracellular cysteine protease expressed by<jats:italic>Streptococcus pyogenes<\/jats:italic>(group A<jats:italic>Streptococcus<\/jats:italic>[GAS]) is a critical virulence factor in a mouse model of invasive disease (S. Lukomski, S. Sreevatsan, C. Amberg, W. Reichardt, M. Woischnik, A. Podbielski, and J. M. Musser, J. Clin. Invest. 99:2574\u20132580, 1997). To facilitate further investigations of the streptococcal cysteine protease, recombinant proteins composed of a 40-kDa zymogen containing a C192S amino acid substitution that ablates enzymatic activity, a 28-kDa mature protein with the C192S replacement, and a 12-kDa propeptide were purified from<jats:italic>Escherichia coli<\/jats:italic>containing His tag expression vectors. The recombinant C192S zymogen retained apparently normal structural integrity, as assessed by the ability of purified wild-type streptococcal cysteine protease to process the 40-kDa molecule to the 28-kDa mature form. All three recombinant purified proteins retained immunologic reactivity with polyclonal and monoclonal antibodies. Humans with a diverse range of invasive disease episodes (erysipelas, cellulitis, pneumonia, bacteremia, septic arthritis, streptococcal toxic shock syndrome, and necrotizing fasciitis) caused by six distinct M types of GAS seroconverted to the streptococcal cysteine protease. These results demonstrate that this GAS protein is expressed in vivo during the course of human infections and thereby provide additional evidence that the cysteine protease participates in host-pathogen interactions in some patients.<\/jats:p>","DOI":"10.1128\/iai.66.2.765-770.1998","type":"journal-article","created":{"date-parts":[[2019,12,31]],"date-time":"2019-12-31T15:23:07Z","timestamp":1577805787000},"page":"765-770","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":48,"title":["Expression and Characterization of Group A<i>Streptococcus<\/i>Extracellular Cysteine Protease Recombinant Mutant Proteins and Documentation of Seroconversion during Human Invasive Disease Episodes"],"prefix":"10.1128","volume":"66","author":[{"given":"Siddeswar","family":"Gubba","sequence":"first","affiliation":[{"name":"<!--label omitted: 1-->Institute for the Study of Human Bacterial Pathogenesis, Department of Pathology, Baylor College of Medicine, Houston, Texas 77030,1 and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Donald E.","family":"Low","sequence":"additional","affiliation":[{"name":"<!--label omitted: 2-->Department of Microbiology, Mount Sinai Hospital, Toronto, Ontario, Canada2"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James M.","family":"Musser","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Institute for the Study of Human Bacterial Pathogenesis, Department of Pathology, Baylor College of Medicine, Houston, Texas 77030,1 and"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.270.17.9862"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1038\/337385a0"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1128\/iai.64.11.4744-4750.1996"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1128\/iai.65.5.1956-1959.1997"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1084\/jem.81.6.573"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1084\/jem.92.3.201"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1084\/jem.85.3.305"},{"key":"e_1_3_2_9_2","first-page":"221","article-title":"Isolation and characterization of erythrogenic toxins. V. identity of erythrogenic toxin type B and streptococcal proteinase precursor.","volume":"255","author":"Gerlach D.","year":"1983","unstructured":"Gerlach D. Knoll H. Kohler W. Ozegowski J. H. Hribalova V. Isolation and characterization of erythrogenic toxins. V. identity of erythrogenic toxin type B and streptococcal proteinase precursor. Zentralbl. Bakteriol. Mikrobiol. Hyg. Abt. Orig. A 255 1983 221 233","journal-title":"Zentralbl. Bakteriol. Mikrobiol. Hyg. Abt. Orig. A"},{"key":"e_1_3_2_10_2","unstructured":"Gubba S. and J. M. Musser. Unpublished data."},{"key":"e_1_3_2_11_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.172.8.4536-4542.1990"},{"key":"e_1_3_2_12_2","doi-asserted-by":"publisher","DOI":"10.1084\/jem.184.2.665"},{"key":"e_1_3_2_13_2","doi-asserted-by":"publisher","DOI":"10.1093\/infdis\/166.1.31"},{"key":"e_1_3_2_14_2","doi-asserted-by":"publisher","DOI":"10.1006\/mpat.1994.1044"},{"key":"e_1_3_2_15_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.90.16.7676"},{"key":"e_1_3_2_16_2","doi-asserted-by":"publisher","DOI":"10.1006\/mpat.1993.1083"},{"key":"e_1_3_2_17_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(18)97551-4"},{"key":"e_1_3_2_18_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(19)83988-1"},{"key":"e_1_3_2_19_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.66.2.771-776.1998"},{"key":"e_1_3_2_20_2","doi-asserted-by":"publisher","DOI":"10.1172\/JCI119445"},{"key":"e_1_3_2_21_2","unstructured":"Musser J. M. Streptococcal superantigen mitogenic factor and pyrogenic exotoxin B expressed by Streptococcus pyogenes . Structure and function Superantigens. Molecular biology immunology and relevance to human disease. Leung D. Y. M. Huber B. T. Schlievert P. M. 1997 281 310 Marcel Dekker Inc. New York N.Y"},{"key":"e_1_3_2_22_2","unstructured":"Musser J. M. and R. M. Krause. The revival of group A streptococcal diseases with a commentary on staphylococcal toxic shock syndrome. In R. M. Krause (ed.) Emerging infections in press. Academic Press Inc. San Diego Calif."},{"key":"e_1_3_2_23_2","doi-asserted-by":"publisher","DOI":"10.1128\/iai.64.6.1913-1917.1996"},{"key":"e_1_3_2_24_2","doi-asserted-by":"crossref","first-page":"396","DOI":"10.4049\/jimmunol.81.5.396","article-title":"The determination of streptococcal antiproteinase titers in sera of patients with rheumatic fever and streptococcal infection.","volume":"81","author":"Ogburn C. A.","year":"1958","unstructured":"Ogburn C. A. Harris T. N. Harris S. The determination of streptococcal antiproteinase titers in sera of patients with rheumatic fever and streptococcal infection. J. Immunol. 81 1958 396 403","journal-title":"J. Immunol."},{"key":"e_1_3_2_25_2","first-page":"3","article-title":"Sur la question de la proteinase streptococcique.","volume":"9","author":"Rotta J.","year":"1957","unstructured":"Rotta J. Sur la question de la proteinase streptococcique. G. Mal. Infett. Parassit. 9 1957 3 8","journal-title":"G. Mal. Infett. Parassit."},{"key":"e_1_3_2_26_2","doi-asserted-by":"publisher","DOI":"10.1128\/iai.64.3.870-877.1996"},{"key":"e_1_3_2_27_2","doi-asserted-by":"publisher","DOI":"10.1084\/jem.94.5.363"},{"key":"e_1_3_2_28_2","unstructured":"Simor A. E. Louie L. Schwartz B. McGeer A. Scriver S. the Ontario GAS Study Project Low D. E. Association of protease activity with group A streptococcal (GAS) necrotizing fasciitis (NF) abstr. 1164. Program and Abstracts of the 33rd Interscience Conference on Antimicrobial Agents and Chemotherapy. 1993 American Society for Microbiology Washington D.C"},{"key":"e_1_3_2_29_2","doi-asserted-by":"publisher","DOI":"10.1084\/jem.85.6.591"}],"container-title":["Infection and Immunity"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/IAI.66.2.765-770.1998","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/IAI.66.2.765-770.1998","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,9,24]],"date-time":"2023-09-24T14:34:09Z","timestamp":1695566049000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.asm.org\/doi\/10.1128\/IAI.66.2.765-770.1998"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1998,2]]},"references-count":28,"journal-issue":{"issue":"2","published-print":{"date-parts":[[1998,2]]}},"alternative-id":["10.1128\/IAI.66.2.765-770.1998"],"URL":"https:\/\/doi.org\/10.1128\/iai.66.2.765-770.1998","relation":{},"ISSN":["0019-9567","1098-5522"],"issn-type":[{"value":"0019-9567","type":"print"},{"value":"1098-5522","type":"electronic"}],"subject":[],"published":{"date-parts":[[1998,2]]},"assertion":[{"value":"1997-06-30","order":0,"name":"received","label":"Received","group":{"name":"publication_history","label":"Publication History"}},{"value":"1997-11-21","order":1,"name":"accepted","label":"Accepted","group":{"name":"publication_history","label":"Publication History"}},{"value":"1998-02-01","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}