Glycosylation of measles virus haemagglutinin protein in infected cells

Ogura, Hisashi; Sato, Hiroshi; Kamiya, Shigeru; Nakamura, Shinichi

doi:10.1099/0022-1317-72-11-2679

Cited by 21 publications

(12 citation statements)

References 21 publications

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“…1B). Whereas the stability of H Edm -ER was similar to that observed for H Edm , H Edm -ER lacked the Golgi-specific conversion from core to complex N-linked oligosaccharide chains characterized by an ϳ4 kDa increase in molecular mass over time (33), suggesting its inhibited export from the ER. This was further assessed by treating the samples corresponding to 180-min chase time with endoglycosidase H (Endo H) prior to immunoblotting (Fig.…”

Section: Glycoproteins Carrying Er Retention Signals At Theirsupporting

confidence: 58%

Measles Virus Envelope Glycoproteins Hetero-oligomerize in the Endoplasmic Reticulum

Plemper

Hammond

Cattaneo

2001

Journal of Biological Chemistry

123

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The endoplasmic reticulum (ER) was investigated as the initial oligomerization site for the envelope glycoproteins H and F of measles virus (MV), a clinically relevant member of the Paramyxoviridae family, and consequences of this interaction for viral replication were studied. Both proteins were tagged at their cytosolic tails with RRR and KKXX motifs, respectively, resulting in their efficient retention in the ER. Cotransfection of the retained constructs with transport competent MV glycoproteins revealed a dominant negative effect on their biological activity indicating intracellular complex formation and thus retention. Pulse-chase analysis and co-immunoprecipitation experiments demonstrated that this effect is based on both homo-and hetero-oligomerization in the ER. Recombinant viruses additionally expressing ERretained F showed an altered cytopathic phenotype accompanied by greatly reduced particle release. Similar mutant viruses additionally expressing ERretained H could not be rescued indicating an even greater negative effect of this protein on virus viability. Our study suggests that both homo-and heterooligomerization of MV glycoproteins occur in the ER and that these events are of significance for early steps of particle assembly.

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Section: Glycoproteins Carrying Er Retention Signals At Theirsupporting

confidence: 58%

Measles Virus Envelope Glycoproteins Hetero-oligomerize in the Endoplasmic Reticulum

Plemper

Hammond

Cattaneo

2001

Journal of Biological Chemistry

123

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“…Similar observations have been made for simian immunodeficiency virus gpl20 expressed by a recombinant vaccinia virus and in MV (Edmonston strain) expression in HeLa cells (Ogura et al, 1991;Spies & Compans, 1993).…”

Section: Characterization Of a Secreted Form Of Measles Virus Haemaggsupporting

confidence: 68%

Characterization of a secreted form of measles virus haemagglutinin expressed from a vaccinia virus recombinant

Malvoisin

Wild

1994

Journal of General Virology

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The measles virus (MV) haemagglutinin (HA) is a class 2 glycoprotein by means of which the virus particle attaches to the host cell receptor. We have previously expressed this glycoprotein as a vaccinia recombinant virus and have shown that the HA glycoprotein synthesized is indistinguishable from that coded by MV. In the present study, we report that in RK13 cells a soluble form (sHA) of the HA is secreted into the medium. We show by SDS-PAGE and sucrose density gradient centrifugation that the sHA is a dimer and is smaller than the cell-associated form. Using a variety of inhibitors the production of sHA was shown to be a late event, probably occurring at the membrane; only fully glycosylated molecules were found in sHA. Finally, we demonstrate that sHA retains its antigenicity with conformation-dependent MAbs and its receptor recognition function. We conclude that sHA is a valuable tool for use in studies of the structure and function of the MV HA glycoprotein.

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“…The heterogeneity in glycosylation is therefore unlikely to be host cell-dependent, but is an intrinsic property dictated by the primary amino acid sequence of the H protein. Two types of H protein caused by altered glycosylation processing have also been observed in virus-infected ceils (Graves, 1981;Ogura et al, 1991). Thus, heterogeneity in H protein glycosylation probably also exists in virus lyric infections.…”

Section: Discussionmentioning

confidence: 99%

Role of N-linked Oligosaccharide Chains in the Processing and Antigenicity of Measles Virus Haemagglutinin Protein

Cattaneo

Schwartz

et al. 1994

Journal of General Virology

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Glycosylation of measles virus haemagglutinin protein in infected cells

Cited by 21 publications

References 21 publications

Measles Virus Envelope Glycoproteins Hetero-oligomerize in the Endoplasmic Reticulum

Measles Virus Envelope Glycoproteins Hetero-oligomerize in the Endoplasmic Reticulum

Characterization of a secreted form of measles virus haemagglutinin expressed from a vaccinia virus recombinant

Role of N-linked Oligosaccharide Chains in the Processing and Antigenicity of Measles Virus Haemagglutinin Protein

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