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Titolo:
IDENTIFICATION OF NEUTRALIZING EPITOPES ON PSEUDOMONAS-AERUGINOSA ELASTASE AND EFFECTS OF CROSS-REACTIONS ON OTHER THERMOLYSIN-LIKE PROTEASES
Autore:
KOOI C; HODGES RS; SOKOL PA;
Indirizzi:
UNIV CALGARY,HLTH SCI CTR,DEPT MICROBIOL & INFECT DIS CALGARY AB T2N 4N1 CANADA UNIV CALGARY,HLTH SCI CTR,DEPT MICROBIOL & INFECT DIS CALGARY AB T2N 4N1 CANADA UNIV ALBERTA,DEPT BIOCHEM EDMONTON AB T6G 2H7 CANADA
Titolo Testata:
Infection and immunity
fascicolo: 2, volume: 65, anno: 1997,
pagine: 472 - 477
SICI:
0019-9567(1997)65:2<472:IONEOP>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
CHOLERAE HEMAGGLUTININ PROTEASE; NUCLEOTIDE-SEQUENCE; ALKALINE PROTEASE; 3-DIMENSIONAL STRUCTURE; MONOCLONAL-ANTIBODIES; GENE; ZINC; PROTEINS; LASA; CEPACIA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
27
Recensione:
Indirizzi per estratti:
Citazione:
C. Kooi et al., "IDENTIFICATION OF NEUTRALIZING EPITOPES ON PSEUDOMONAS-AERUGINOSA ELASTASE AND EFFECTS OF CROSS-REACTIONS ON OTHER THERMOLYSIN-LIKE PROTEASES", Infection and immunity, 65(2), 1997, pp. 472-477

Abstract

Monoclonal antibodies (MAbs) to a Burkholderia (Pseudomonas) cepacia 36-kDa protease (PSCP) which neutralize PSCP and Pseudomonas aeruginosa elastase but not P. aeruginosa alkaline protease have been isolated (C. Kooi et al., Infect. Immun, 62:2811-2817, 1994). These MAbs, designated 36-6-6 and 36-6-8, react with N-chlorosuccinimide cleavage products of P. aeruginosa elastase, consistent with the recognition of a 13.9-kDa fragment which contains the active site, Overlapping 9-mer peptides that span this region were synthesized, Neutralizing MAbs to PSCPreacted strongly with two peptides ((341)HGFTEQNSG(349) and (395)RYM DQPSRD(403)). Peptide (341)HGFTEQNSG(349) overlaps the motif (337)HEXXH(341), which has been found in many zinc-dependent endopeptidases. Peptide (395)RYMDQPSRD(403) lies between E(361), which binds a zinc atoln, and H-420, which acts as a proton donor at the active site, Polyclonal rabbit sera raised against these peptides reacted with elastase onWestern immunoblots and by enzyme-linked immunosorbent assay, With hide powder azure as the substrate, antisera to either HGFTEQNG and RYMDQPSRD completely neutralized the activities of elastase, thermolysin, Vibrio cholerae hemagglutinin/protease, and PSCP but had no effect on P. aeruginosa alkaline protease or the Serratia marcescens major protease. These results suggest that the MAbs recognize two different epitopes on P. aeruginosa elastase and that antibodies raised against synthetic peptides corresponding to either of these epitopes neutralize proteolytic activity.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/11/20 alle ore 13:35:55