{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,26]],"date-time":"2026-09-26T03:04:27Z","timestamp":1790391867941,"version":"4.1.0"},"reference-count":42,"publisher":"Microbiology Society","issue":"9","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2005,9,1]]},"abstract":"<jats:p><jats:italic>Neisseria gonorrhoeae<\/jats:italic>releases monomeric peptidoglycan (PG) fragments during growth. These PG fragments affect pathogenesis-related phenotypes including induction of inflammatory cytokines and killing of ciliated fallopian tube cells. Although the biological activities of these molecules have been established in multiple systems, the genes and gene products responsible for their production in<jats:italic>N. gonorrhoeae<\/jats:italic>have not been determined. The authors previously identified genes for three lytic transglycosylase homologues (<jats:italic>ltgA<\/jats:italic>,<jats:italic>ltgB<\/jats:italic>and<jats:italic>ltgC<\/jats:italic>) in the<jats:italic>N. gonorrhoeae<\/jats:italic>genome sequence. Mutation of<jats:italic>ltgA<\/jats:italic>was found to affect PG fragment release, and mutation of<jats:italic>ltgC<\/jats:italic>affected cell separation. In this study the effects of complete deletion or point mutations in<jats:italic>ltgB<\/jats:italic>were characterized. Point mutations were introduced by a combination of insertion-duplication mutagenesis and positive and negative selection, thereby generating selectable marker-less mutations. The<jats:italic>ltgB<\/jats:italic>deletion mutant had normal growth characteristics and was not affected in PG fragment release. When expressed in<jats:italic>Escherichia coli<\/jats:italic>, gonococcal LtgB was able to substitute for lambda endolysin to cause cell lysis. Mutation of the predicted catalytic-site glutamic acid residue did not decrease lysis in this system. However, mutation of a nearby glutamic acid residue eliminated lysis activity.<\/jats:p>","DOI":"10.1099\/mic.0.28125-0","type":"journal-article","created":{"date-parts":[[2005,9,8]],"date-time":"2005-09-08T22:34:01Z","timestamp":1126218841000},"page":"3081-3088","source":"Crossref","is-referenced-by-count":15,"title":["Characterization of the role of LtgB, a putative lytic transglycosylase in Neisseria gonorrhoeae"],"prefix":"10.1099","volume":"151","author":[{"given":"Petra L.","family":"Kohler","sequence":"first","affiliation":[{"name":"Department of Medical Microbiology and Immunology, University of Wisconsin-Madison Medical School, Madison, 1300 University Avenue, 471A MSC, WI 53706, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Karen A.","family":"Cloud","sequence":"additional","affiliation":[{"name":"Department of Medical Microbiology and Immunology, University of Wisconsin-Madison Medical School, Madison, 1300 University Avenue, 471A MSC, WI 53706, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kathleen T.","family":"Hackett","sequence":"additional","affiliation":[{"name":"Department of Medical Microbiology and Immunology, University of Wisconsin-Madison Medical School, Madison, 1300 University Avenue, 471A MSC, WI 53706, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eric T.","family":"Beck","sequence":"additional","affiliation":[{"name":"Department of Medical Microbiology and Immunology, University of Wisconsin-Madison Medical School, Madison, 1300 University Avenue, 471A MSC, WI 53706, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joseph P.","family":"Dillard","sequence":"additional","affiliation":[{"name":"Department of Medical Microbiology and Immunology, University of Wisconsin-Madison Medical School, Madison, 1300 University Avenue, 471A MSC, WI 53706, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"345","reference":[{"key":"R1","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1007\/BF00271205","article-title":"The R gene product of bacteriophage lambda is the murein transglycosylase","volume":"184","author":"Bienkowska-Szewczyk","year":"1981","journal-title":"Mol Gen Genet"},{"key":"R2","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1007\/s002390010136","article-title":"Identification of four families of peptidoglycan lytic transglycosylases","volume":"52","author":"Blackburn","year":"2001","journal-title":"J Mol Evol"},{"key":"R3","doi-asserted-by":"crossref","first-page":"464","DOI":"10.1093\/infdis\/167.2.464","article-title":"The biological activities of peptidoglycan in experimental Haemophilus influenzae meningitis","volume":"167","author":"Burroughs","year":"1993","journal-title":"J Infect Dis"},{"key":"R4","first-page":"877","article-title":"Peptidoglycan-degrading enzymes in ether-treated cells of Neisseria gonorrhoeae","volume":"129","author":"Chapman","year":"1983","journal-title":"J Gen Microbiol"},{"key":"R5","doi-asserted-by":"crossref","first-page":"2752","DOI":"10.1128\/IAI.70.6.2752-2757.2002","article-title":"A lytic transglycosylase of Neisseria gonorrhoeae is involved in peptidoglycan-derived cytotoxin production","volume":"70","author":"Cloud","year":"2002","journal-title":"Infect Immun"},{"key":"R6","doi-asserted-by":"crossref","first-page":"7811","DOI":"10.1128\/JB.186.22.7811-7814.2004","article-title":"Mutation of a single lytic transglycosylase causes aberrant septation and inhibits cell separation of Neisseria gonorrhoeae","volume":"186","author":"Cloud","year":"2004","journal-title":"J Bacteriol"},{"key":"R7","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1089\/mdr.1996.2.141","article-title":"Identification of new members of the lytic transglycosylase family in Haemophilus influenzae and Escherichia coli","volume":"2","author":"Dijkstra","year":"1996","journal-title":"Microb Drug Resist"},{"key":"R8","doi-asserted-by":"crossref","first-page":"810","DOI":"10.1016\/0959-440X(94)90261-5","article-title":"\u2018Holy\u2019 proteins. 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