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Functional analysis of the sialic acid-binding adhesin SfaS of pathogenic Escherichia coli by site-specific mutagenesis.
The gene coding for the sialic acid-specific adhesin SfaS produced by the S fimbrial adhesin (sfa) determinant of Escherichia coli has been modified by oligonucleotide-directed, site-specific mutagenesis. Lysine 116, arginine 118, and lysine 122 were replaced by threonine, serine, and threonine, res...
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| Опубликовано в: : | Infect Immun |
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| Главные авторы: | , , , |
| Формат: | Artigo |
| Язык: | Inglês |
| Опубликовано: |
American Society for Microbiology (ASM)
1990
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| Предметы: | |
| Online-ссылка: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC258787/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/2194961/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/iai.58.7.2133-2138.1990 |
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