Recombinant Platelet Membrane Glycoprotein IV (GP4)
The exact identification of the HIV-1 envelope glycoprotein (Env) liable for productive medical an infection might be instrumental in elucidating the molecular foundation of HIV-1 transmission and in designing efficient vaccines.
Right here, we developed a mathematical mannequin of random viral evolution and, along with phylogenetic tree building, used it to investigate 3,449 full env sequences derived by single genome amplification from 102 topics with acute HIV-1 (clade B) an infection.
Viral env genes evolving from particular person transmitted or founder viruses typically exhibited a Poisson distribution of mutations and star-like phylogeny, which coalesced to an inferred consensus sequence at or close to the estimated time of virus transmission. General, 78 of 102 topics had proof of productive medical an infection by a single virus, and 24 others had proof of productive medical an infection by a minimal of two to 5 viruses.
Phenotypic evaluation of transmitted or early founder Envs revealed a constant sample of CCR5 dependence, masking of coreceptor binding areas, and equal or modestly enhanced resistance to the fusion inhibitor T1249 and broadly neutralizing antibodies in contrast with Envs from chronically contaminated topics.
Low multiplicity an infection and restricted viral evolution previous peak viremia counsel a finite window of potential vulnerability of HIV-1 to vaccine-elicited immune responses, though phenotypic properties of transmitted Envs pose a formidable protection.
Hemagglutinin (HA) is the receptor-binding and membrane fusion glycoprotein of influenza virus and the goal for infectivity-neutralizing antibodies.
The constructions of three conformations of the ectodomain of the 1968 Hong Kong influenza virus HA have been decided by X-ray crystallography: the single-chain precursor, HA0; the metastable neutral-pH conformation discovered on virus, and the fusion pH-induced conformation.
These constructions present a framework for designing and deciphering the outcomes of experiments on the exercise of HA in receptor binding, the technology of rising and reemerging epidemics, and membrane fusion throughout viral entry. Buildings of HA in advanced with sialic acid receptor analogs, along with binding experiments, present particulars of those low-affinity interactions by way of the sialic acid substituents acknowledged and the HA residues concerned in recognition.
Neutralizing antibody-binding websites encompass the receptor-binding pocket on the membrane-distal floor of HA, and the constructions of the complexes between neutralizing monoclonal Fabs and HA point out potential neutralization mechanisms.
Cleavage of the biosynthetic precursor HA0 at a outstanding loop in its construction primes HA for subsequent activation of membrane fusion at endosomal pH (Determine 1).
Priming entails insertion of the fusion peptide right into a charged pocket within the precursor; activation requires its extrusion in direction of the fusion goal membrane, because the N terminus of a newly fashioned trimeric coiled coil, and repositioning of the C-terminal membrane anchor close to the fusion peptide on the similar finish of a rod-shaped molecule.
Comparability of this new HA conformation, which has been fashioned for membrane fusion, with the constructions decided for different virus fusion glycoproteinsmeans that these molecules are all within the fusion-activated conformation and that the juxtaposition of the membrane anchor and fusion peptide, a recurring function, is concerned within the fusion mechanism.
Extension of those comparisons to the soluble N-ethyl-maleimide-sensitive issue attachment protein receptor (SNARE) protein advanced of vesicle fusion permits an analogous conclusion.
Description: Human Osteoactivin, His Tag (GPB-H5229) is expressed from human 293 cells (HEK293). It contains AA Ala 22 - Pro 486 (Accession # AAH32783).
The envelope glycoprotein of human immunodeficiency virus type 1 (HIV-1) consists of a complex of gp120 and gp41. gp120 determines viral tropism by binding to target-cell receptors, while gp41 mediates fusion between viral and cellular membranes.
Previous studies identified an alpha-helical domain within gp41 composed of a trimer of two interacting peptides. The crystal structure of this complex, composed of the peptides N36 and C34, is a six-helical bundle.
Three N36 helices form an interior, parallel coiled-coil trimer, while three C34 helices pack in an oblique, antiparallel manner into highly conserved, hydrophobic grooves on the surface of this trimer.
This structure shows striking similarity to the low-pH-induced conformation of influenza hemagglutinin and likely represents the core of fusion-active gp41. Avenues for the design/discovery of small-molecule inhibitors of HIV infection are directly suggested by this structure.
Human Platelet Membrane Glycoprotein IIb/IIIa (GPIIb/IIIa) CLIA Package
Human immunodeficiency virus-type 1 (HIV-1) entry requires fusion cofactors on the CD4+ goal cell. Fusin, a heterotrimeric GTP-binding protein (G protein)-coupled receptor, serves as a cofactor for T cell line-tropic isolates. The chemokines RANTES, MIP-1alpha, and MIP-1beta, which suppress an infection by macrophage-tropic isolates, selectively inhibited cell fusion mediated by the corresponding envelope glycoproteins (Envs).
Recombinant CC CKR5, a G protein-coupled receptor for these chemokines, rendered CD4-expressing nonhuman cells fusion-competent preferentially with macrophage-tropic Envs.
CC CKR5 messenger RNA was detected selectively in cell varieties inclined to macrophage-tropic isolates. CC CKR5 is thus a fusion cofactor for macrophage-tropic HIV-1 strains.
Description: A polyclonal antibody against GPNMB. Recognizes GPNMB from Human, Mouse. This antibody is Unconjugated. Tested in the following application: ELISA, IHC
Description: A polyclonal antibody for detection of GPNMB from Human, Mouse, Rat. This GPNMB antibody is for WB, ELISA. It is affinity-purified from rabbit serum by affinity-chromatography using the specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from part region of human GPNMB protein
Description: A polyclonal antibody for detection of GPNMB from Human, Mouse, Rat. This GPNMB antibody is for WB, ELISA. It is affinity-purified from rabbit serum by affinity-chromatography using the specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from part region of human GPNMB protein
Description: A polyclonal antibody for detection of GPNMB from Human, Mouse, Rat. This GPNMB antibody is for WB, ELISA. It is affinity-purified from rabbit serum by affinity-chromatography using the specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from part region of human GPNMB protein
Description: The protein encoded by this gene is a type I transmembrane glycoprotein which shows homology to the pMEL17 precursor, a melanocyte-specific protein. GPNMB shows expression in the lowly metastatic human melanoma cell lines and xenografts but does not show expression in the highly metastatic cell lines. GPNMB may be involved in growth delay and reduction of metastatic potential. Two transcript variants encoding different isoforms have been found for this gene.
Description: The protein encoded by this gene is a type I transmembrane glycoprotein which shows homology to the pMEL17 precursor, a melanocyte-specific protein. GPNMB shows expression in the lowly metastatic human melanoma cell lines and xenografts but does not show expression in the highly metastatic cell lines. GPNMB may be involved in growth delay and reduction of metastatic potential. Two transcript variants encoding different isoforms have been found for this gene.
Description: The protein encoded by this gene is a type I transmembrane glycoprotein which shows homology to the pMEL17 precursor, a melanocyte-specific protein. GPNMB shows expression in the lowly metastatic human melanoma cell lines and xenografts but does not show expression in the highly metastatic cell lines. GPNMB may be involved in growth delay and reduction of metastatic potential. Two transcript variants encoding different isoforms have been found for this gene.
