Abstract |
Neisseria gonorrhoeae encodes five lytic transglycosylases (LTs) in the core genome, and most gonococcal strains also carry the gonococcal genetic island that encodes one or two additional LTs. These peptidoglycan (PG)-degrading enzymes are required for a number of processes that are either involved in the normal growth of the bacteria or affect the pathogenesis and gene transfer aspects of this species that make N. gonorrhoeae highly inflammatory and highly genetically variable. Systematic mutagenesis determined that two LTs are involved in producing the 1,6-anhydro PG monomers that cause the death of ciliated cells in Fallopian tubes. Here, we review the information available on these enzymes and discuss their roles in bacterial growth, cell separation, autolysis, type IV secretion, and pathogenesis.
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Authors | Yolande A Chan, Kathleen T Hackett, Joseph P Dillard |
Journal | Microbial drug resistance (Larchmont, N.Y.)
(Microb Drug Resist)
Vol. 18
Issue 3
Pg. 271-9
(Jun 2012)
ISSN: 1931-8448 [Electronic] United States |
PMID | 22432703
(Publication Type: Journal Article, Research Support, N.I.H., Extramural, Review)
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Chemical References |
- Bacterial Proteins
- Isoenzymes
- Peptide Fragments
- Peptidoglycan
- Glycosyltransferases
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Topics |
- Bacterial Proteins
(chemistry, genetics, metabolism)
- Cilia
(drug effects, microbiology)
- Epithelial Cells
(drug effects, microbiology, pathology)
- Fallopian Tubes
(drug effects, microbiology, pathology)
- Female
- Glycosyltransferases
(chemistry, genetics, metabolism)
- Gonorrhea
(microbiology, pathology)
- Humans
- Isoenzymes
(chemistry, genetics, metabolism)
- Mutagenesis
- Mutation
- Neisseria gonorrhoeae
(enzymology, genetics, pathogenicity)
- Peptide Fragments
(metabolism, pharmacology)
- Peptidoglycan
(metabolism, pharmacology)
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