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Sequence variation in two ipaH genes of Shigella flexneri 5 and homology to the LRG‐like family of proteins
Author(s) -
Venkatesan M. M.,
Buysse J. M.,
Hartman A. B.
Publication year - 1991
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1991.tb02089.x
Subject(s) - biology , shigella flexneri , homology (biology) , gene , genetics , sequence analysis , recombinant dna , plasmid , peptide sequence , microbiology and biotechnology , conserved sequence , amino acid , southern blot , escherichia coli
Summary Oligonucleotide primers derived from the ipaH 7.8 sequence have been used to determine the boundaries of DNA sequence homology among five lpaH genes on the invasion plasmid (pWR100) of Shigella flexneri 5, strain M9OT‐W. The primary structure of lpaH 4.5 has been established from DNA sequence analysis. The first 197 amino acids in lpaH 7.8 were replaced in lpaH 4.5 by a unique set of 251 amino acids, generating two related proteins with variable and conserved sequences. The amino‐terminal region of lpaH 4.5 displayed an internal repeat structure, also seen in lpaH 7.8 , characteristic of members of the leucine‐rich glycoprotein (LRG) family. The DNA sequences of ipaH 2.5 and ipaH 1.4 indicate that these genes are truncated versions of lpaH 7.8 . Western blot analysis of a λgt11 ipaH recombinant (W7) subclone demonstrated that the antigenicity of lpaH 7.8 resides outside the leucine‐rich repetitive region.