Multimerization potential of the cytoplasmic domain of the human cytomegalovirus glycoprotein B

Scheffczik, Hanno; Kraus, Ina; Kiermayer, Simone; Bogner, Elke; Holzenburg, Andreas; Garten, Wolfgang; Eickmann, Markus

doi:10.1016/s0014-5793(01)02891-5

FEBS Letters

2001

DOI: 10.1016/s0014-5793(01)02891-5

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Multimerization potential of the cytoplasmic domain of the human cytomegalovirus glycoprotein B

Hanno Scheffczik¹,

Ina Kraus²,

Simone Kiermayer³

et al.

Abstract: In the present study the coding sequence of the cytoplasmic tail of the human cytomegalovirus glycoprotein B (gB) was expressed. The secondary structure of the purified recombinant protein was analyzed by circular dichroism, and the quaternary structure was investigated by gel permeation chromatography, and electron microscopy. Our data indicate that the cytoplasmic gB domain contains K K-helix structures and assembles into tetramers, suggesting that the authentic gB may represent a homotetramer. ß

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Site directed mutagenesis of the carboxyl terminus of human cytomegalovirus glycoprotein B leads to attenuation of viral growth in cell culture

et al. 2004

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A viable human cytomegalovirus (HCMV) mutant was generated harbouring a glycoprotein B (gB) in which the carboxyl-terminal amino acids DRLRHR (aa 885-900) were changed to AALREE. Characterization of the phenotype of the recombinant virus revealed significant reduction of infectious progeny release and only moderate reduction of viral DNA replication indicating its diminished specific infectivity. This observation was in line with immunogold labeling of extracellular virions demonstrating that the amount of gB protein was markedly reduced in the envelope of the mutant virus. Our results suggest that the conserved carboxyl-terminus of the gB molecule is critical for HCMV maturation.

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Site directed mutagenesis of the carboxyl terminus of human cytomegalovirus glycoprotein B leads to attenuation of viral growth in cell culture

et al. 2004

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Human Cytomegalovirus Binding to DC-SIGN Is Required for Dendritic Cell Infection and Target Cell trans-Infection

et al. 2002

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Cytomegalovirus (CMV) infection is characterized by host immunosuppression and multiorganic involvement. CMV-infected dendritic cells (DC) were recently shown to display reduced immune functions, but their role in virus dissemination is not clear. In this report, we demonstrated that CMV could be captured by DC through binding on DC-SIGN and subsequently transmitted to permissive cells. Moreover, blocking DC-SIGN by specific antibodies inhibited DC infection by primary CMV isolates and expression of DC-SIGN or its homolog DC-SIGNR rendered susceptible cells permissive to CMV infection. We demonstrated that CMV envelope glycoprotein B is a viral ligand for DC-SIGN and DC-SIGNR. These results provide new insights into the molecular interactions contributing to cell infection by CMV and extend DC-SIGN implication in virus propagation.

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Multimerization potential of the cytoplasmic domain of the human cytomegalovirus glycoprotein B

Cited by 2 publications

References 26 publications

Site directed mutagenesis of the carboxyl terminus of human cytomegalovirus glycoprotein B leads to attenuation of viral growth in cell culture

Site directed mutagenesis of the carboxyl terminus of human cytomegalovirus glycoprotein B leads to attenuation of viral growth in cell culture

Human Cytomegalovirus Binding to DC-SIGN Is Required for Dendritic Cell Infection and Target Cell trans-Infection

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