PMID- 15140992
OWN - NLM
STAT- MEDLINE
DCOM- 20040610
LR  - 20240322
IS  - 0022-538X (Print)
IS  - 1098-5514 (Electronic)
IS  - 0022-538X (Linking)
VI  - 78
IP  - 11
DP  - 2004 Jun
TI  - Mutational analyses of Epstein-Barr virus glycoprotein 42 reveal functional 
      domains not involved in receptor binding but required for membrane fusion.
PG  - 5946-56
AB  - Epstein-Barr virus (EBV) is a human gammaherpesvirus associated with malignancies 
      of both epithelial and lymphoid origin. Efficient infection of the latent host 
      reservoir B lymphocytes involves the binding of glycoproteins gp350/220 for 
      initial attachment, followed by the concerted action of gH, gL, gB, and gp42 for 
      membrane fusion. The type II membrane protein gp42 is required for infection of B 
      cells and assembles into a complex with gH and gL. The cellular host receptor for 
      gp42, class II human leukocyte antigen (HLA), has been structurally verified by 
      crystallization analyses of gp42 bound to HLA-DR1. Interestingly, the crystal 
      structure revealed a hydrophobic pocket consisting of many aromatic and aliphatic 
      residues from the predicted C-type lectin domain of gp42 that in other members of 
      the C-type lectin family binds major histocompatibility complex class I or other 
      diverse ligands. Although the hydrophobic pocket does not bind HLA class II, 
      mutational analyses presented here indicate that this domain is essential for 
      EBV-induced membrane fusion. In addition, mutational analysis of the region of 
      gp42 contacting HLA class II in the gp42-HLA-DR1 cocrystal confirms that this 
      region interacts with HLA class II and that this interaction is also important 
      for EBV-induced membrane fusion.
FAU - Silva, Amanda L
AU  - Silva AL
AD  - Department of Microbiology and Immunology, Northwestern University Medical 
      School, Ward 6-231, Chicago, IL 60611, USA.
FAU - Omerovic, Jasmina
AU  - Omerovic J
FAU - Jardetzky, Theodore S
AU  - Jardetzky TS
FAU - Longnecker, Richard
AU  - Longnecker R
LA  - eng
GR  - GM61050/GM/NIGMS NIH HHS/United States
GR  - R01 CA093444/CA/NCI NIH HHS/United States
GR  - R01 AI038972/AI/NIAID NIH HHS/United States
GR  - R01 GM061050/GM/NIGMS NIH HHS/United States
GR  - T32 GM08061/GM/NIGMS NIH HHS/United States
GR  - R56 AI038972/AI/NIAID NIH HHS/United States
GR  - T32 GM008061/GM/NIGMS NIH HHS/United States
GR  - R01 CA062234/CA/NCI NIH HHS/United States
GR  - R01 DE013127/DE/NIDCR NIH HHS/United States
GR  - CA62234/CA/NCI NIH HHS/United States
GR  - CA93444/CA/NCI NIH HHS/United States
GR  - R01 CA073507/CA/NCI NIH HHS/United States
GR  - CA73507/CA/NCI NIH HHS/United States
GR  - AI38972/AI/NIAID NIH HHS/United States
GR  - DE13127/DE/NIDCR NIH HHS/United States
GR  - R37 AI038972/AI/NIAID NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Virol
JT  - Journal of virology
JID - 0113724
RN  - 0 (Glycoproteins)
RN  - 0 (Histocompatibility Antigens Class II)
RN  - 0 (Receptors, Virus)
RN  - 0 (Viral Proteins)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Binding Sites
MH  - CHO Cells
MH  - Cricetinae
MH  - Glycoproteins/*chemistry/physiology
MH  - Histocompatibility Antigens Class II/analysis/metabolism
MH  - *Membrane Fusion
MH  - Molecular Sequence Data
MH  - Receptors, Virus/*physiology
MH  - Viral Proteins/*chemistry/physiology
PMC - PMC415818
EDAT- 2004/05/14 05:00
MHDA- 2004/06/21 10:00
PMCR- 2004/06/01
CRDT- 2004/05/14 05:00
PHST- 2004/05/14 05:00 [pubmed]
PHST- 2004/06/21 10:00 [medline]
PHST- 2004/05/14 05:00 [entrez]
PHST- 2004/06/01 00:00 [pmc-release]
AID - 78/11/5946 [pii]
AID - 2284-03 [pii]
AID - 10.1128/JVI.78.11.5946-5956.2004 [doi]
PST - ppublish
SO  - J Virol. 2004 Jun;78(11):5946-56. doi: 10.1128/JVI.78.11.5946-5956.2004.