The Carboxy-Terminal 18 Amino Acids of the Measles Virus Hemagglutinin Are Essential for Its Biological Function

Blain, F.; Liston, Peter; Briedis, Dalius J.

doi:10.1006/bbrc.1995.2418

Cited by 5 publications

(1 citation statement)

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“…Glycosylation is essential for proper folding and intracellular transport from the Golgi. In the binding of protein H to its receptor 18C-terminal residues are involved ( [67], and reviewed in [66]). …”

Section: H Proteinmentioning

confidence: 99%

Role of sialic acid-containing molecules in paramyxovirus entry into the host cell: A minireview

2006

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Sialic acid-containing compounds play a key role in the initial steps of the paramyxovirus life cycle. As enveloped viruses, their entry into the host cell consists of two main events: binding to the host cell and membrane fusion. Virus adsorption occurs at the surface of the host cell with the recognition of specific receptor molecules located at the cell membrane by specific viral attachment proteins. The viral attachment protein present in some paramyxoviruses (Respirovirus, Rubulavirus and Avulavirus) is the HN glycoprotein, which binds to cellular sialic acid-containing molecules and exhibits sialidase and fusion promotion activities. Gangliosides of the gangliotetraose series bearing the sialic acid N-acetylneuraminic (Neu5Ac) on the terminal galactose attached in alpha2-3 linkage, such as GD1a, GT1b, and GQ1b, and neolacto-series gangliosides are the major receptors for Sendai virus. Much less is known about the receptors for other paramyxoviruses than for Sendai virus. Human parainfluenza viruses 1 and 3 preferentially recognize oligosaccharides containing N-acetyllactosaminoglycan branches with terminal Neu5Acalpha2-3Gal. In the case of Newcastle disease virus, has been reported the absence of a specific pattern of the gangliosides that interact with the virus. Additionally, several works have described the use of sialylated glycoproteins as paramyxovirus receptors. Accordingly, the design of specific sialic acid analogs to inhibit the sialidase and/or receptor binding activity of viral attachment proteins is an important antiviral strategy. In spite of all these data, the exact nature of paramyxovirus receptors, apart from their sialylated nature, and the mechanism(s) of viral attachment to the cell surface are poorly understood.

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Section: H Proteinmentioning

confidence: 99%

Role of sialic acid-containing molecules in paramyxovirus entry into the host cell: A minireview

2006

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Structural and Functional Studies of the Measles Virus Hemagglutinin: Identification of a Novel Site Required for CD46 Interaction

et al. 1999

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The entry of measles virus (MV) into human cells is mediated by the initial attachment of the viral hemagglutinin (HA) to the complement regulatory protein CD46. Two subdomains, one each within CD46 short consensus repeats (SCRs) 1 and 2, are responsible for this interaction. However, little is known about the regions within MV HA needed for a high-affinity CD46 interaction. To better define the HA-CD46 interaction, we took three approaches: chimeric domain swapping, peptide scanning, and alanine scanning mutagenesis. Chimeras of MV HA and the closely related rinderpest virus (RPV) HA were generated and tested for cell surface expression and the ability to hemadsorb CD46+ red blood cells (RBC). Exchanges with the N terminus of RPV were tolerated as MV HA could be replaced with RPV HA up to amino-acid position 154. However, both larger swaps with RPV and a small RPV HA replacement at the C terminus aborted cell-surface expression. Peptide scanning with 51 overlapping peptides derived from three MV HA regions showed one peptide, corresponding to MV HA amino acids 468-487, blocked hemagglutination of African green monkey (AGM) RBCs and inhibited MV infection of Chinese hamster ovary cells (CHO) expressing human CD46. Alanine scanning mutants mapped sites on the MV HA that were not required for trafficking to the cell surface or function in hemagglutination as well as a novel site required for CD46 interaction, amino acids 473-477.

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Molecular biology of the morbilliviruses

Barrett¹,

Banyard²,

Diallo³

2006

Rinderpest and Peste Des Petits Ruminants

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The Carboxy-Terminal 18 Amino Acids of the Measles Virus Hemagglutinin Are Essential for Its Biological Function

Cited by 5 publications

References 0 publications

Role of sialic acid-containing molecules in paramyxovirus entry into the host cell: A minireview

Role of sialic acid-containing molecules in paramyxovirus entry into the host cell: A minireview

Structural and Functional Studies of the Measles Virus Hemagglutinin: Identification of a Novel Site Required for CD46 Interaction

Molecular biology of the morbilliviruses

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