title: Epstein-Barr virus glycoprotein gM can interact with the cellular protein p32 and knockdown of p32 impairs virus.
abstract: The Epstein-Barr virus glycoprotein complex gMgN has been implicated in assembly and release of fully enveloped virus, although the precise role that it plays has not been elucidated. We report here that the long predicted cytoplasmic tail of gM is not required for complex formation and that it interacts with the cellular protein p32, which has been reported to be involved in nuclear egress of human cytomegalovirus and herpes simplex virus. Although redistribution of p32 and colocalization with gM was not observed in virus infected cells, knockdown of p32 expression by siRNA or lentivirus-delivered shRNA recapitulated the phenotype of a virus lacking expression of gNgM. A proportion of virus released from cells sedimented with characteristics of virus lacking an intact envelope and there was an increase in virus trapped in nuclear condensed chromatin. The observations suggest the possibility that p32 may also be involved in nuclear egress of Epstein-Barr virus.
authors.affiliation: Department of Microbiology and Immunology, Center for Molecular and Tumor Virology and Feist-Weiller Cancer Center, Louisiana State University Health Sciences Center, Shreveport, LA, USA.
authors.forename: Harish
authors.initials: H
authors.lastname: Changotra
authors.affiliation: Department of Microbiology and Immunology, Center for Molecular and Tumor Virology and Feist-Weiller Cancer Center, Louisiana State University Health Sciences Center, Shreveport, LA, USA.
authors.forename: Susan M
authors.initials: SM
authors.lastname: Turk
authors.affiliation: Department of Biochemistry, University of Kansas Medical Center, Kansas City, KS, USA.
authors.forename: Antonio
authors.initials: A
authors.lastname: Artigues
authors.affiliation: Department of Microbiology and Immunology, Center for Molecular and Tumor Virology and Feist-Weiller Cancer Center, Louisiana State University Health Sciences Center, Shreveport, LA, USA.
authors.forename: Nagendra
authors.initials: N
authors.lastname: Thakur
authors.affiliation: Department of Microbiology and Immunology, Center for Molecular and Tumor Virology and Feist-Weiller Cancer Center, Louisiana State University Health Sciences Center, Shreveport, LA, USA.
authors.forename: Mindy
authors.initials: M
authors.lastname: Gore
authors.affiliation: Department of Microbiology and Immunology, Center for Molecular and Tumor Virology and Feist-Weiller Cancer Center, Louisiana State University Health Sciences Center, Shreveport, LA, USA.
authors.forename: Martin I
authors.initials: MI
authors.lastname: Muggeridge
authors.affiliation: Department of Microbiology and Immunology, Center for Molecular and Tumor Virology and Feist-Weiller Cancer Center, Louisiana State University Health Sciences Center, Shreveport, LA, USA. Electronic address: lhuttf@lsuhsc.edu.
authors.forename: Lindsey M
authors.initials: LM
authors.lastname: Hutt-Fletcher
mesh_terms: D020816:Amino Acid Motifs; D020031:Epstein-Barr Virus Infections / Q000235:genetics / Q000378:metabolism* / Q000821:virology; D004854:Herpesvirus 4, Human / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D011485:Protein Binding; D014759:Viral Envelope Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
chemical_list: D014759:Viral Envelope Proteins; C000608767:glycoprotein M, human herpesvirus 4
keywords: Epstein–Barr virus; Glycoprotein gM; Glycoprotein gN; Virus egress; p32