نتایج جستجو برای: zinc metalloprotease

تعداد نتایج: 76334  

2016
Mani H. Vemula Raghavender Medisetti Rakesh Ganji Kiran Jakkala Swetha Sankati Kiranam Chatti Sharmistha Banerjee

Zinc metalloprotease-1 (Zmp1) from Mycobacterium tuberculosis (M.tb), the tuberculosis (TB) causing bacillus, is a virulence factor involved in inflammasome inactivation and phagosome maturation arrest. We earlier reported that Zmp1 was secreted under granuloma-like stress conditions, induced Th2 cytokine microenvironment and was highly immunogenic in TB patients as evident from high anti-Zmp1 ...

Journal: :PLoS Pathogens 2007
Paul M Grandgenett Keiko Otsu Helen R Wilson Mary E Wilson John E Donelson

The Trypanosoma brucei genome encodes three groups of zinc metalloproteases, each of which contains approximately 30% amino acid identity with the major surface protease (MSP, also called GP63) of Leishmania. One of these proteases, TbMSP-B, is encoded by four nearly identical, tandem genes transcribed in both bloodstream and procyclic trypanosomes. Earlier work showed that RNA interference aga...

Journal: :Infection and immunity 2000
J M Fakruddin S Biswas Y D Sharma

The malaria parasite affects millions of people each year, lives and multiplies in two different hosts, and synthesizes a large number of proteases and heat shock proteins (HSPs) for its survival. We describe here the characterization of a metalloprotease activity which resides in the small HSP (PVHSP28) of the common but noncultivable human malaria parasite Plasmodium vivax. The protein is exp...

Journal: :Infection and immunity 2002
Frédéric Brouta Frédéric Descamps Michel Monod Sandy Vermout Bertrand Losson Bernard Mignon

Keratinolytic proteases secreted by dermatophytes are likely to be virulence-related factors. Microsporum canis, the main agent of dermatophytosis in dogs and cats, causes a zoonosis that is frequently reported. Using Aspergillus fumigatus metalloprotease genomic sequence (MEP) as a probe, three genes (MEP1, MEP2, and MEP3) were isolated from an M. canis genomic library. They presented a quite-...

Journal: :Journal of bacteriology 1994
S Ayora P E Lindgren F Götz

Two extracellular proteases from Staphylococcus hyicus subsp. hyicus, ShpI and ShpII, have been characterized. ShpI is a neutral metalloprotease with broad substrate specificity; the gene has been cloned and sequenced. ShpII, characterized here, is mainly produced in the late logarithmic growth phase in contrast to ShpI, which is mainly produced in the late stationary growth phase. ShpII was pu...

Journal: :Transfusion 2002
Han-Mou Tsai

Thrombotic thrombocytopenic purpura, characterized by the presence of systemic hyaline thrombi in the arterioles and capillaries, is a potentially fatal disease that responds to plasma infusion or exchange. Recent studies have demonstrated that a metalloprotease in the normal plasma cleaves endothelial von Willebrand factor to a series of multimers. A deficiency of the protease, due to autoimmu...

Journal: :Infection and immunity 2006
C Kooi B Subsin R Chen B Pohorelic P A Sokol

In previous studies we characterized the Burkholderia cenocepacia ZmpA zinc metalloprotease. In this study, we determined that B. cenocepacia has an additional metalloprotease, which we designated ZmpB. The zmpB gene is present in the same species as zmpA and was detected in B. cepacia, B. cenocepacia, B. stabilis, B. ambifaria, and B. pyrrocinia but was absent from B. multivorans, B. vietnamie...

2017
Saraspadee Mootien Paul M Kaplan

We have developed 22 mouse IgG1 monoclonal antibodies (mAbs) against Bacteroides fragilis zinc metalloprotease toxins 1 and 2 (BFT1 and BFT2). Mice were immunized with recombinant BFT1 or BFT2 proteins with metalloprotease activity. Eight of the mAbs bind specifically to BFT1. One mAb, 2H6, binds specifically to BFT2. The remaining 13 mAbs bind to both BFT1 and BFT2. The eight BFT1-specific mAb...

Journal: :Fish & shellfish immunology 2010
Yannick Labreuche Frédérique Le Roux Joël Henry Céline Zatylny Arnaud Huvet Christophe Lambert Philippe Soudant Didier Mazel Jean-Louis Nicolas

Extracellular products (ECPs) of the pathogenic Vibrio aestuarianus 01/32 were previously reported to display lethality in Crassostrea gigas oysters and to cause morphological changes and immunosuppression in oyster hemocytes. To identify the source of this toxicity, biochemical and genetic approaches were developed. ECP protease activity and lethality were shown to be significantly reduced fol...

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