Zobrazeno 1 - 10
of 49
pro vyhledávání: '"W R, McMaster"'
Autor:
Akram Miramin Mohammadi, Liv Eidsmo, Thorsten Lieke, Susanne Nylén, Hannah Akuffo, Louise Berg, W. R. McMaster, Ali Khamesipour
Publikováno v:
Clinical and Experimental Immunology. 153:221-230
SummaryNatural killer (NK) cells contribute to immunity as the first line of defence in numerous infections by early cytokine secretion and cytotoxicity. In Leishmania infection, NK cells contribute with interferon-γ and may assist in directing the
Publikováno v:
Experimental Parasitology. 100:44-53
The protozoan parasite Leishmania has a digenetic life cycle, alternating between the promastigote and the amastigote stages. Amastigotes infect macrophage cells and reside in the hydrolytic environment of the phagolysosome. Leishmania show distinct
Publikováno v:
Scandinavian Journal of Immunology. 54:414-420
Objectives of this study were to test the cytokine gene expression in peripheral blood mononuclear cells (PBMCs) from cases with nonhealing and healing cutaneous leishmaniasis (CL) in response to in vitro stimulation of recombinant gp63 (rgp63) and s
Autor:
Anne Dell, W R McMaster, Charlotte J. Morrison, Richard L. Easton, Howard R. Morris, James M. Piret
Publikováno v:
Biotechnology and Bioengineering. 68:407-421
The N-linked glycans of recombinant leishmanolysin (GP63) expressed as a glycosylphosphatidylinositol (GPI)-anchored membrane protein or modified for secretion in Chinese hamster ovary (CHO) cells were analyzed by fast atom bombardment-mass spectrome
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1253:199-207
The major surface glycoprotein of Leishmania promastigotes, referred to as GP63, is a zinc metalloproteinase of 63 000 Mr containing a glycosylphosphatidylinositol (GPI) membrane anchor. Recent studies demonstrated that recombinant GP63 (rGP63) expre
Autor:
Charlotte J. Morrison, Andrew Brittingham, K P Chang, David M. Mosser, W R McMaster, B.S. McGwire
Publikováno v:
The Journal of Immunology. 155:3102-3111
The Leishmania surface protease gp63 has been identified as a parasite virulence factor. To better define the role of gp63 in Leishmania infectivity, the interaction of recombinant gp63 with complement and complement receptors was examined. On Leishm
Publikováno v:
Experimental Parasitology. 78:161-174
Proteins containing tandemly repeating peptide sequences are characteristic of several parasite antigens. Previously it was reported that Leishmania major contain two genes, Lm20 and Lm39, consisting of two unrelated repeat sequences of 42 and 30 bas
Publikováno v:
Parasitology. 108:S29-S36
SUMMARYThe major surface glycoprotein ofLeishmania, referred to as GP63, is a zinc metalloproteinase of 63000Mrpresent on promastigotes and amastigotes from diverse species ofLeishmania. GP63 shares several characteristics with the members of the mat
Publikováno v:
Gene. 134:75-81
A gene encoding the Leishmania surface metalloproteinase, GP63, was modified using the polymerase chain reaction to obtain effective secretion of recombinant GP63 (reGP63) in the baculovirus insect cell expression system. The coding region for the N-
Autor:
J R Webb, W R McMaster
Publikováno v:
Journal of Biological Chemistry. 268:13994-14002
The genes encoding GP63, the major surface glycoprotein of the protozoan parasite Leishmania, are highly conserved across diverse species of Leishmania both within the protein coding region and in the immediate 5'-untranslated region. Located between