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FEMS Immunol Med Microbiol ; 33(2): 77-88, 2002 Jun 03.
Artigo em Inglês | MEDLINE | ID: mdl-12052562

RESUMO

Bacteriolytic activity was detected in extracts of whole mite and spent growth medium (SGM) from the clinically important Dermatophagoides pteronyssinus and Dermatophagoides farinae mites and was most abundant in whole mite extract. Gram-positive organisms Micrococcus lysodeikticus, Bacillus megaterium and Listeria monocytogenes were preferentially lysed and the lytic activity was enhanced by thiols, destroyed by mite proteases, inhibited by HgCl2 and high concentrations of NaCl but was resistant to heat and acid treatment. Substrate SDS-PAGE analysis indicated the presence of several lytic enzymes, two of which were isolated from D. pteronyssinus spent growth medium extract by hydroxyapatite chromatography. The N-terminal amino acid sequence of one of them was then used in PCR-based cloning studies. The complete amino acid sequence of this protein was determined and cDNA found to encode a 130-amino acid residue mature protein with a 20-amino acid leader sequence. The deduced protein demonstrated sequence similarity with the C-terminal regions of a group of bacterial proteins belonging to the P60 superfamily. These data suggest that the enzyme is derived from bacteria within the mites rather than from mites per se.


Assuntos
Bacteriólise , Poeira , Enzimas/isolamento & purificação , Bactérias Gram-Positivas/fisiologia , Ácaros/enzimologia , Sequência de Aminoácidos , Animais , Proteínas de Bactérias/química , Proteínas de Bactérias/genética , Proteínas de Bactérias/isolamento & purificação , Proteínas de Bactérias/metabolismo , Sequência de Bases , Meios de Cultivo Condicionados/química , Meios de Cultivo Condicionados/metabolismo , DNA Complementar , Eletroforese em Gel de Poliacrilamida , Enzimas/química , Enzimas/genética , Enzimas/metabolismo , Bactérias Gram-Positivas/enzimologia , Habitação , Ácaros/microbiologia , Dados de Sequência Molecular
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