GENETIC-CHARACTERIZATION OF BORDETELLA-PERTUSSIS FILAMENTOUS HEMAGGLUTININ - A PROTEIN PROCESSED FROM AN UNUSUALLY LARGE PRECURSOR

被引：98
作者：
DOMENIGHINI, M
RELMAN, D
CAPIAU, C
FALKOW, S
PRUGNOLA, A
SCARLATO, V
RAPPUOLI, R
机构：
[1] STANFORD UNIV,DEPT MICROBIOL & IMMUNOL,STANFORD,CA 94305
[2] SCLAVO RES CTR,I-53100 SIENA,ITALY
[3] SMITH KLINE RECH & IND THERAPEUT SA,B-1330 RIXENSART,BELGIUM
来源：
MOLECULAR MICROBIOLOGY | 1990年 / 4卷 / 05期
关键词：
D O I：
10.1111/j.1365-2958.1990.tb00649.x
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The nucleotide sequence of the structural gene for filamentous haemagglutinin (FHA), fhaB, a crucial adherence factor for Bordetella perfussis, has been determined. Its 10774 nucleotides are far more than necessary to encode the 220kD biologically active, mature polypeptide product, suggesting a role for co‐or post‐translational processing. Fusion proteins derived from various portions of the fhaB open reading frame (ORF) were used to generate polyclonal antisera. Western immunoblot analysis of purified FHA and Bordetella sp. whole cell extracts with these antisera indicated that the 220kD product is encoded by the 5 portion of the ORF and that the smaller polypeptide species are breakdown products of this polypeptide. These data, as well as N‐terminal amino acid sequencing of the major polypeptide species, suggest a scheme for the proteolytic processing of an FHA precursor polypeptide. Copyright © 1990, Wiley Blackwell. All rights reserved
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页码：787 / 800
页数：14
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