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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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