Conserved lipoprotein H.8 of pathogenicNeisseriaconsists entirely of pentapeptide repeats
作者:
J. P. Woods,
S. M. Spinola,
S. M. Strobel,
J. G. Cannon,
期刊:
Molecular Microbiology
(WILEY Available online 1989)
卷期:
Volume 3,
issue 1
页码: 43-48
ISSN:0950-382X
年代: 1989
DOI:10.1111/j.1365-2958.1989.tb00102.x
出版商: Blackwell Publishing Ltd
数据来源: WILEY
摘要:
SummaryThe pathogenicNeisseria, N. gonorrhoeaeandN. meningitidis, possess an outer membrane protein (OMP), designated H.8, with a conserved monoclonal antibody (MAb)‐binding epitope. We determined the DNA sequence of a gonococcal H.8 gene, and confirmed the relationship between the cloned gene and the H.8 OMP by constructing a gonococcal mutant lacking H.8. The predicted H.8 OMP is a lipoprotein 71 amino acids in length, composed of 13 repeats of a consensus sequence AAEAP with perfect 5‐residue periodicity. The AAEAP units form a repeating epitope that comprises the entire predicted sequence of the prot
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