Oral Norovirus Infection Is Blocked in Mice Lacking Peyer's Patches and Mature M Cells.
Ann Arbor, United States. In J Virol, 2014
To define the importance of Peyer's patch (PP) M cells during MNV pathogenesis, we used a model of BALB/c mice deficient in recombination-activating gene 2 (Rag2) and the common gamma chain (γc) (Rag-γc(-/-)), which lack gut-associated lymphoid tissues (GALT), such as Peyer's patches, and mature GP2(+) M cells.
Isolation and Genetic Analysis of Multidrug Resistant Bacteria from Diabetic Foot Ulcers.
Benares, India. In Front Microbiol, 2014
In addition to the presence of class 1 integron, six β-lactamase resistance encoding genes namely bla TEM, bla SHV, bla OXA, bla CTX-M-gp1, bla CTX-M-gp2, and bla CTX-M-gp9 and two methicillin resistance genes namely mecA and femA and vancomycin resistance encoding genes (vanA and vanB) were identified in different isolates.
Serological studies in inflammatory bowel disease: how important are they?
Budapest, Hungary. In Curr Opin Gastroenterol, 2014
Anti-Saccharomyces cerevisiae antibody remains the most accurate single marker, and recently identified exocrine pancreas antibodies (GP2 and CUZD1) have been suggested as evidence for a role of antibodies in the pathogenesis of Crohn's disease.
Glycoprotein 2 antibodies in Crohn's disease.
Senftenberg, Germany. In Adv Clin Chem, 2012
Utilizing immunoblotting and matrix-assisted laser desorption ionization time-of-flight mass spectrometry, the major zymogen granule membrane glycoprotein 2 (GP2) has been discovered as the main PAB autoantigen.
Small molecule inhibitors reveal Niemann-Pick C1 is essential for Ebola virus infection.
Boston, United States. In Nature, 2011
Combined with the results of previous studies of GP structure and function, our findings support a model of EboV infection in which cleavage of the GP1 subunit by endosomal cathepsin proteases removes heavily glycosylated domains to expose the amino-terminal domain, which is a ligand for NPC1 and regulates membrane fusion by the GP2 subunit.
The ZP domain is a conserved module for polymerization of extracellular proteins.
New York City, United States. In Nat Cell Biol, 2002
Among these proteins are the mammalian sperm receptors ZP2 and ZP3, non-mammalian egg coat proteins, Tamm-Horsfall protein (THP), glycoprotein-2 (GP-2), alpha- and beta-tectorins, transforming growth factor (TGF)-beta receptor III and endoglin, DMBT-1 (deleted in malignant brain tumour-1), NompA (no-mechanoreceptor-potential-A), Dumpy and cuticlin-1 (refs 1,2).