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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제19권 제9호
- 발행연도
- 2009.1
- 수록면
- 932 - 945 (14page)
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초록· 키워드
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Several species of Gram-positive bacteria have cell wall
peptidoglycan (syn. murein) in which not all of the sugar
moieties are N-acetylated. This has recently been shown to
be a secondary effect, caused by the action of a peptidoglycan
N-acetylglucosamine deacetylase. We have found that the
opportunistic pathogen Listeria monocytogenes is unusual
in having three enzymes with such activity, two of which
remain in the cytoplasm. Here, we examine the enzyme
(PgdA) that crosses the cytoplasmic membrane and is
localized in the cell wall. We purified a hexa-His-tagged
form of PgdA to study its activity and constructed a
mutant devoid of functional Lmo0415 (PgdA) protein.
L. monocytogenes PgdA protein exhibited peptidoglycan
N-acetylglucosamine deacetylase activity with natural
substrates (peptidoglycan) from both L. monocytogenes
and Escherichia coli as well as the peptidoglycan sugar
chain component N-acetylglucosamine, but not with
N-acetylmuramic acid. As was reported recently [6],
inactivation of the structural gene was not lethal for
L. monocytogenes nor did it affect growth rate or morphology
of the cells. However, the pgdA mutant was more prone to
autolysis induced by such agents as Triton X-100 and
EDTA, and is more susceptible to the cationic antimicrobial
peptides (CAMP) lysozyme and mutanolysin, using either
peptidoglycan muramidases or autolysis-inducing agents.
The pgdA mutant was also slightly more susceptible than
the wild-type strain to the action of certain beta-lactam
antibiotics. Our results indicate that protein PgdA plays a
protective physiological role for listerial cells.
목차
등록된 정보가 없습니다.
참고문헌 (24)
참고문헌 신청
Arnold, K., L. / 2006 / The SWISS-MODEL Workspace: A Web-based environment for protein structure homology modelling / Bioinformatics 22 : 195 ~ 201
Baj, J. / 1992 / N-Unsubstituted glucosamine residues and other modifications in murein of the obligatory chemolithotroph Thiobacillus neapolitanus / Res. Microbiol 143 : 47
Bera, A. / 2006 / The presence of peptidoglycan O-acetyltransferase in various staphylococcal species correlates with lysozyme resistance and pathogenicity / Infect. Immun 74
Bishop, J. L. / 2007 / Deception point: Peptidoglycan modification as a means of immune evasion / Proc. Natl. Acad. Sci. U.S.A. 104 : 691 ~ 692
Bohne, J. / 1996 / Differential regulation of the virulence genes of Listeria monocytogenes by the transcriptional activator PrfA / Mol. Microbiol 20 : 1189 ~ 1198
Baj, J. / 1992 / N-Unsubstituted glucosamine residues and other modifications in murein of the obligatory chemolithotroph Thiobacillus neapolitanus / Res. Microbiol 143 : 47
Bera, A. / 2006 / The presence of peptidoglycan O-acetyltransferase in various staphylococcal species correlates with lysozyme resistance and pathogenicity / Infect. Immun 74
Bishop, J. L. / 2007 / Deception point: Peptidoglycan modification as a means of immune evasion / Proc. Natl. Acad. Sci. U.S.A. 104 : 691 ~ 692
Bohne, J. / 1996 / Differential regulation of the virulence genes of Listeria monocytogenes by the transcriptional activator PrfA / Mol. Microbiol 20 : 1189 ~ 1198
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