The predicted primary structure of the measles virus hemagglutinin

Alkhatib, Ghalib; Briedis, Dalius J.

doi:10.1016/0042-6822(86)90312-0

Cited by 146 publications

(73 citation statements)

References 28 publications

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“…The nucleotide sequences of cloned cDNAs corresponding to the full-length MV H mRNA indicate that five potential N-linked glycosylation sites are present on the MV H protein (Alkhatib & Briedis, 1986). Individual N-linked oligosaccharide chains of the simian virus 5 HN protein have recently been reported to have different roles in its folding, assembly and transport (Ng et al, 1990).…”

Section: Discussionmentioning

confidence: 99%

Glycosylation of measles virus haemagglutinin protein in infected cells

Ogura¹,

Sato²,

Kamiya³

et al. 1991

Journal of General Virology

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Section: Discussionmentioning

confidence: 99%

Glycosylation of measles virus haemagglutinin protein in infected cells

Ogura¹,

Sato²,

Kamiya³

et al. 1991

Journal of General Virology

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“…Furthermore, animals immunized with vaccinia virus expressing the H protein are protected from a lethal challenge with intracerebral inoculation of MV (Drillien et al, 1988). The nucleotide sequence of the H gene has been determined (Alkhatib & Briedis, 1986;Gerald et al, 1986). The predicted M r of the H protein is about 69K.…”

Section: Introductionmentioning

confidence: 99%

Role of individual cysteine residues in the processing and antigenicity of the measles virus haemagglutinin protein

Norrby²

1994

Journal of General Virology

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The haemagglutinin (H) protein is the dominant envelope glycoprotein of measles virus. The protein contains 13 cysteine residues among its 617 amino acids and all are located in its ectodomain. In previous studies, the capacity of a panel of monoclonal antibodies (MAbs) to react with continuous and discontinuous epitopes was defined. It was shown that the absence of disulphide bonds impaired the capacity of the protein to react with MAbs specific for the discontinuous epitopes. In the present study, our objective was to determine the contribution of individual cysteine residues to the folding of H protein into its native conformation. Site-directed oligonucleotide mutagenesis was used to create 13 mutants, each with a serine replacing a cysteine. The mutated genes were directly expressed in the BHK-21 cells by use of a vaccinia virus-driven T7 polymerase system. Investigations of the antigenic structure and intracellular processing properties of the mutant proteins reveal the following outcome. (i) Replacements of cysteine residues 139, 154, 188,386, 570 or 606 had no detectable effect on the antigenic structure and intracellular processing of the H protein. However, a mutant with a replaced cysteine residue 154 displayed modified migration properties. (ii) Alterations of cysteine residues 381 or 494 displayed a moderate effect on H protein properties. The two mutants expressed discontinuous epitopes, indicating that they were partially folded, but they did not oligomerize, did not reach the medial Golgi complex and failed to be transported to the cell surface. (iii) Substitutions of cysteine residues 287, 300, 394, 579 or 583 resulted in a complete loss of binding of the MAbs that recognize the discontinuous epitopes, with no effect on the binding of a MAb reacting with a continuous epitope. No dimeric form of the proteins was observed and only high mannose oligosaccharides were demonstrated in these mutants, suggesting that the modified proteins did not oligomerize and were retained in the endoplasmic reticulum. In conclusion, cysteine residues 287, 300, 381,394, 494, 579 and 583 appear to play a particularly critical role in the antigenic structure and processing of the H molecules and they probably participate in the inter-or intramolecular disulphide bonding.

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“…MV H cDNAs were then amplified by PCR using °Tth' DNA polymerase (Toyobo Co., Ltd.) and appropriate sets of primers over 35 cycles each consisting of 1 min at 94 °C, 2 min at 50 °C and 3 min at 72 °C. Sequences of the primers used in the present study were chosen based on the reported sequences (Alkhatib & Briedis, 1986;Gerald et al, 1986) Nucleotide sequence analysis. Amplified DNA fragments were subcloned into the M13mpl9 vector and sequenced by the dideoxynucleotide chain termination method (Sanger et al, 1977) using the Sequenase DNA sequence kit (United States Biochemical).…”

Section: Reverse Transcription-pcr (Rt-pcr)mentioning

confidence: 99%

Increased binding activity of measles virus to monkey red blood cells after long-term passage in Vero cell cultures

Shibahara

Hotta

Katayama

et al. 1994

Journal of General Virology

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Recent field isolates of measles virus (MV) obtained by using B95-8 cells have been reported not to agglutinate African green monkey red blood cells (AGM-RBC). Vero cell-adapted, plaque-forming strains derived from three field isolates at the third passage in Vero cell cultures (T8Ve-3, T11Ve-3 and N13Ve-3) also exhibited markedly decreased binding activity, as determined by infectivity-absorption and haemadsorption tests. On the other hand, binding activity of the respective strains at the twentieth passage

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The predicted primary structure of the measles virus hemagglutinin

Cited by 146 publications

References 28 publications

Glycosylation of measles virus haemagglutinin protein in infected cells

Glycosylation of measles virus haemagglutinin protein in infected cells

Role of individual cysteine residues in the processing and antigenicity of the measles virus haemagglutinin protein

Increased binding activity of measles virus to monkey red blood cells after long-term passage in Vero cell cultures

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