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Titolo:
A point mutation in the active site of Legionella pneumophila O-acetyltransferase results in modified lipopolysaccharide but does not influence virulence
Autore:
Luck, CP; Freier, T; Steudel, C; Knirel, YA; Luneberg, E; Zahringer, U; Helbig, JH;
Indirizzi:
Tech Univ Dresden, Inst Med Mikrobiol & Hyg, D-01307 Dresden, Germany TechUniv Dresden Dresden Germany D-01307 Hyg, D-01307 Dresden, Germany Forschungszentrum, Zentrum Expt Biol & Biowissensch, D-23845 Borstel, Germany Forschungszentrum Borstel Germany D-23845 nsch, D-23845 Borstel, Germany Russian Acad Sci, ND Zelinskii Organ Chem Inst, Moscow 117913, Russia Russian Acad Sci Moscow Russia 117913 n Chem Inst, Moscow 117913, Russia Univ Wurzburg, Inst Hyg & Mikrobiol, D-97080 Wurzburg, Germany Univ Wurzburg Wurzburg Germany D-97080 robiol, D-97080 Wurzburg, Germany
Titolo Testata:
INTERNATIONAL JOURNAL OF MEDICAL MICROBIOLOGY
fascicolo: 5, volume: 291, anno: 2001,
pagine: 345 - 352
SICI:
1438-4221(200111)291:5<345:APMITA>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
COMPLETE GENOME SEQUENCE; MONOCLONAL-ANTIBODIES; SEROGROUP-1 STRAINS; INTRACELLULAR MULTIPLICATION; MOLECULAR CHARACTERIZATION; HUMAN MACROPHAGES; LOCUS; GENE; CLONING; ACANTHAMOEBA;
Keywords:
Legionella pneumophila serogroup 1; lipopolysaccharide mutant; monoclonal antibodies; intracellular multiplication;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
39
Recensione:
Indirizzi per estratti:
Indirizzo: Luck, CP Tech Univ Dresden, Inst Med Mikrobiol & Hyg, Fiedlerstr 42, D-01307 Dresden, Germany Tech Univ Dresden Fiedlerstr 42 Dresden Germany D-01307 Germany
Citazione:
C.P. Luck et al., "A point mutation in the active site of Legionella pneumophila O-acetyltransferase results in modified lipopolysaccharide but does not influence virulence", INT J MED M, 291(5), 2001, pp. 345-352

Abstract

The majority of clinical isolates of Legionella pneumophila serogroup 1 produce lipopolysaccharide (LPS) that reacts with monoclonal antibody (MAb) 3/1. By using a negative cell sorting method, we isolated a spontaneous LPS mutant from L. pneumophila serogroup I strain Corby that lost reactivity with this MAb. The mutant contained a single nucleotide exchange in position 169 of the lag-1 gene that encodes an O-acetyltransferase that is responsible for O-acetylation of the L. pneumophila O-repeat unit (legionaminic acid). This mutation resulted in a single amino acid exchange in a highly conserved motif present in many O-acetyltransferase-like proteins. RT-PCR analysis revealed that the mutant lag-1 gene was transcribed, but the resulting protein lacked O-acetyltransferase activity. Chemical analysis of the mutantLPS revealed that it lacked 8-O-acetyl groups in legionaminic acid. In addition, the mutant failed to produce high-molecular-weight long-chain O-polysaccharide. Complementation of the mutant with the wild-type lag-1 gene restored reactivity with MAb 3/1 and the chemical structure of the wild-type LPS. Strain Corby and its MAb 3/1-negative mutant were indistinguishable in their serum resistance characteristics, and in uptake and intracellular multiplication in Acanthamoeba castellanii and macrophages.

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Documento generato il 06/04/20 alle ore 11:31:07