Alterations induced by penicillin in the protein profile and cell structure of Group GStreptococcus |
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Authors: | de Castro Angela Christina Dias Meirelles Maria Nazareth Leal Hampshire de Carvalho Santos Angela Vieira Veronica V Leite Luis Henrique Rocha Travassos Luis Rodolpho Vermelho Alane Beatriz |
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Institution: | (1) Department of Medical Microbiology, Federal University of Rio de Janeiro, Brazil;(2) Department of General Microbiology, Federal University of Rio de Janeiro, Brazil;(3) Department of Ultrastructure and Cell Biology, FIOCRUZ, Rio de Janeiro, Brazil;(4) Department of Cell Biology, EPM, São Paulo, Brazil;(5) Instituto de Microbiologia, CCS, Bloco I. Universidade Federal do Rio de Janeiro, Cidade Universitária, Ilha do Fundão, 21941 Rio de Janeiro, RJ, Brasil |
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Abstract: | We investigated the effect of a subminimal concentration of penicillin on the ultrastructure and protein profile of Group G streptococci. In cells treated with penicillin (1/3 MIC), the protein content increased by 50%, and several protein bands with a molecular mass of 14–70 kDa were detected. In the hydrophilic phase, carbohydrate-containing proteins were detected by PAS staining, and in the hydrophobic phase, a group of proteins that reacted strongly with homologous antisera were observed. In terms of cell structure, Triton X-114 extraction was found to induce alterations in the cross wall of untreated cells. In bacteria treated with penicillin but not extracted with Triton X-114, the cell wall was observed to detach itself, and regions with reduced amounts of cellular material appeared in the cytoplasm. After Triton-X114 extraction, these penicillin-treated cells exhibited profound morphological changes, leading in some cases to lysis. |
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