Disease relevance of H

• Induction of subacute murine measles encephalitis by monoclonal antibody to virus haemagglutinin [1].
• Haemagglutinin of measles virus: purification and storage with preservation of biological and immunological properties [2].
• A total of 24 monoclonal antibodies (MAbs) against the haemagglutinin (H) and the fusion protein (F) of rinderpest virus (RPV) were used to characterize their antigenic structure and biological properties, and to analyse natural variation in the envelope proteins of morbilliviruses [3].
• Characterization of a secreted form of measles virus haemagglutinin expressed from a vaccinia virus recombinant [4].
• CD9-dependent regulation of Canine distemper virus-induced cell-cell fusion segregates with the extracellular domain of the haemagglutinin [5].

High impact information on H

• We report here that a monoclonal antibody directed against the virus haemagglutinin, unlike an antibody to the virus nucleocapsid protein, is able to induce a subacute encephalitis in vivo [1].
• It was investigated whether this effect was restricted to only one viral glycoprotein, either the haemagglutinin (H) or the fusion (F) protein, which form a fusion complex on the surface of virions and infected cells, or whether it is dependent on both in transient co-transfection assays [5].
• Characterization of this recombinant virus revealed that the N481Y substitution in the haemagglutinin allowed it to utilize CD46 as an alternative receptor, but that its ability to use CD46 was rather low in CD46+ SLAM- cell lines compared with that of the recombinant virus possessing the haemagglutinin of the Edmonston laboratory strain [6].
• The recombinant MV, based on a SLAM-using clinical isolate in which asparagine at position 481 of the haemagglutinin was replaced with tyrosine, was generated [6].
• The cell surface expression of MV fusion (F), but not haemagglutinin, envelope protein resulted in complement activation of the Factor B-dependent alternative pathway in a dose-dependent manner and F-C3b complexes were formed [7].

Chemical compound and disease context of H

• Immune and artificial selection in the haemagglutinin (H) glycoprotein of measles virus [8].
• Measles virus haemagglutinin (H), fusion (F) and matrix (M) components were purified by affinity chromatography using monoclonal antibodies coupled to CNBr-activated Sepharose [9].
• Role of individual cysteine residues in the processing and antigenicity of the measles virus haemagglutinin protein [10].
• Oral or parenteral administration of replication-deficient adenoviruses expressing the measles virus haemagglutinin and fusion proteins: protective immune responses in rodents [11].
• Measles virus envelope haemagglutinin (H) was purified rapidly with Triton X-100-solubilized virions by a two-step anion-exchange chromatography using fast protein liquid chromatography [2].

Biological context of H

• Measles virus haemagglutinin gene: cloning, complete nucleotide sequence analysis and expression in COS cells [12].
• Histologically, however, a moderate peribronchitis was observed after immunization with the plasmid expressing the fusion protein whereas, after immunization with plasmids expressing haemagglutinin or both glycoproteins, only mild or focal peribronchitis was seen [13].
• Measles virus genes encoding the haemagglutinin (HA), fusion protein (F) or nucleoprotein (NP) have been inserted into the vaccinia virus genome either alone or in various combinations [14].
• A combined analysis of hydrophilicity, accessibility and flexibility parameters of the deduced amino acid sequence of measles virus (MV) haemagglutinin (H) was used to select 10 regions for synthesis of 10- or 11-amino acid-long peptides [15].
• The ability of MV wild-type strains in particular to infect DCs in vitro is dearly established, and the receptor binding haemagglutinin protein of these viruses essentially determines this particular tropism [16].

Anatomical context of H

• To unravel the intracellular fate of measles virus (MV) haemagglutinin (H) following fusion of the virus envelope with the cell membrane, its presentation by MHC molecules to T cells was explored [17].
• The haemagglutinin protein (H) of measles virus (MV) binds to susceptible cells and collaborates with the fusion protein (F) to mediate fusion of the virus with the cell membrane [18].
• Syncytium formation by the mutant that was analysed after coexpression with haemagglutinin protein depended on the presence of trypsin [19].
• This epitope was coupled by (i) a glycine-glycine spacer to a B cell epitope from the fusion protein (residues 404 to 414) and (ii) either its amino or carboxy terminus to a neutralizing antibody epitope from the haemagglutinin (residues 188 to 199) [20].
• The aim of this study was to define the helper T cell epitopes on the haemagglutinin (H) of measles virus (MV) in BALB/c (H-2d) and TO (H-2s) mice [21].

Associations of H with chemical compounds

• A specific response was detected to all RPV proteins tested, namely the haemagglutinin (H), fusion (F), nucleocapsid (N) and matrix (M) proteins, in animals vaccinated with the attenuated strain of the virus [22].
• Cross-linking studies with a variety of chemicals stabilized dimeric forms of the haemagglutinin (HA) or fusion (F) proteins, although by sucrose density gradient analysis, oligomers corresponding to tetramers and larger were observed for both proteins [23].
• Treatment of BGM/MV cells with actinomycin D effected an increase in the percentage of cells expressing cell surface virus haemagglutinin (HA) at times when the percentage of cells with surface HA was less than the percentage of cells with intracellular measles antigens [24].
• We note that the haemagglutinin (H) sequence of D7 viruses shows distinct exchanges of certain amino acids in the stem and propeller domain compared to C2, D6 and the MV vaccine strains used [25].
• We observed no antigenic variation in the haemagglutinin, the fusion glycoprotein, or in the matrix protein [26].

Other interactions of H

• Sequence Analysis of the Haemagglutinin and Fusion Protein Genes of Peste-des-petits Ruminants Vaccine Virus of Indian Origin [27].
• In radioimmunoprecipitation assay, 10 MAbs recognized nucleoprotein, 4 recognized the matrix protein and one each haemagglutinin and phosphoprotein [28].

Analytical, diagnostic and therapeutic context of H

• Vaccine aerosol given either by mask in a dose of 3500 or 7000 plaque-forming units (PFU) or from a plastic bag at a dose of 7000 PFU raised haemagglutinin-inhibiting or plaque-inhibiting measles antibody 16-24 weeks after vaccination to a titre of 1 in 8 or greater in all but 3 of the 51 children so vaccinated [29].
• A total of 35 wild-type measles viruses identified in Victoria, Australia, between 1973 and 1998 were characterized by nucleic acid sequence analysis of the nucleoprotein gene and, in some cases, the haemagglutinin gene [30].
• A membrane immunofluorescence test revealed that the decreased binding activity to AGM-RBC of T8Ve-3, T11Ve-3 and N13Ve-3 was not due to decreased expression of the haemagglutinin (H) protein on the cell surface [31].
• Previously, we have shown that cotton rats are a good animal model to study MV-induced immune suppression, where proliferation inhibition after ex vivo stimulation of cotton rat spleen cells is induced by the viral glycoproteins (fusion and haemagglutinin proteins) [32].
• The antigenic determinants of the haemagglutinin and haemolysin antigens of measles virus were located at the surface of HEp2 cells infected with measles virus and on measles virions released from these cells, using immunoelectron microscopy [33].

References