1. Sequence variation in two ipaH genes of Shigella flexneri 5 and homology to the LRG-like family of proteins.
- Author
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Venkatesan MM, Buysse JM, and Hartman AB
- Subjects
- Amino Acid Sequence, Animals, Base Sequence, Cloning, Molecular, DNA, Bacterial genetics, DNA, Bacterial isolation & purification, Escherichia coli genetics, Humans, Leucine, Molecular Sequence Data, Multigene Family, Oligodeoxyribonucleotides, Plasmids, Restriction Mapping, Sequence Homology, Nucleic Acid, Antigens, Bacterial, Bacterial Proteins genetics, Genes, Bacterial, Genetic Variation, Glycoproteins genetics, Shigella flexneri genetics
- Abstract
Oligonucleotide primers derived from the ipaH7.8 sequence have been used to determine the boundaries of DNA sequence homology among five ipaH genes on the invasion plasmid (pWR100) of Shigella flexneri 5, strain M9OT-W. The primary structure of IpaH4.5 has been established from DNA sequence analysis. The first 197 amino acids in IpaH7.8 were replaced in IpaH4.5 by a unique set of 251 amino acids, generating two related proteins with variable and conserved sequences. The amino-terminal region of IpaH4.5 displayed an internal repeat structure, also seen in IpaH7.8, characteristic of members of the leucine-rich glycoprotein (LRG) family. The DNA sequences of ipaH2.5 and ipaH1.4 indicate that these genes are truncated versions of ipaH7.8. Western blot analysis of a lambda gt11 ipaH recombinant (W7) subclone demonstrated that the antigenicity of IpaH7.8 resides outside the leucine-rich repetitive region.
- Published
- 1991
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