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1.
Virology ; 280(2): 262-72, 2001 Feb 15.
Article in English | MEDLINE | ID: mdl-11162840

ABSTRACT

To determine whether infection with HIV-1 strains of different tropisms would influence expression of the mucosa-associated integrins alpha 4 beta 7 and alpha E beta 7 or the lymph node homing receptor L-selectin on peripheral T lymphocytes, cells were infected with the CXCR4-tropic (X4)/syncytium-inducing (SI) HIV-1(IIIB) strain or with X4/SI or CCR5-tropic (R5)/non-SI (NSI) primary human isolates. Flow cytometric analyses of CD4(+) T cells from cultures infected with HIV-1(IIIB) and one X4/SI primary HIV-1 isolate revealed a significant increase in surface expression of alpha 4 beta 7 and alpha E beta 7 12 days after infection. L-selectin expression was not significantly affected on CD4(+) T cells. However, infection with another X4/SI and two R5/NSI primary HIV-1 isolates did not significantly alter homing receptor expression on CD4(+) T cells. Since a higher degree of CD4 cytopathicity occurred in those cultures having increased integrin expression, these data suggest that significantly altered mucosal homing receptor expression on CD4(+) T cells may result as a "bystander" effect after infection with some cytopathic isolates of HIV-1.


Subject(s)
CD4-Positive T-Lymphocytes/metabolism , HIV Infections/immunology , HIV-1/immunology , Integrins/biosynthesis , L-Selectin/biosynthesis , CD4-Positive T-Lymphocytes/virology , Cells, Cultured , Cytopathogenic Effect, Viral , HIV-1/pathogenicity , HIV-1/physiology , Humans , Mucous Membrane/metabolism
2.
FEMS Microbiol Lett ; 165(1): 123-7, 1998 Aug 01.
Article in English | MEDLINE | ID: mdl-9711848

ABSTRACT

Staphylococcus simulans biovar staphylolyticus produces a staphylolytic glycylglycine endopeptidase (lysostaphin) and a micrococcolytic endo-beta-N-acetylglucosaminidase (hexosaminidase) as proenzymes that are proteolytically processed through multiple intermediates to their mature forms by an extracellular sulfhydryl protease. Analysis of protease production by immunoblots using antiserum prepared against purified protease and by renaturing activity gels using gelatin as the substrate has revealed that the lysostaphin-processing protease also is produced as a proenzyme, which appears to be autocatalytically processed. Very little proprotease could be detected in supernatants from cultures of S. simulans biovar staphylolyticus, which suggested that the protein was being processed before it was released to the culture medium. Analysis of wall-associated proteins revealed that processing of proprotease occurred primarily in the cell wall. Furthermore, processing of prolysostaphin and prohexosaminidase also occurred in the cell wall matrix.


Subject(s)
Cysteine Endopeptidases/metabolism , Enzyme Precursors/metabolism , Hexosaminidases/metabolism , Lysostaphin/metabolism , Staphylococcus/enzymology , Animals , Antibodies, Bacterial , Electrophoresis, Polyacrylamide Gel , Immunoblotting , Membrane Proteins/analysis , Membrane Proteins/isolation & purification , Rabbits
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