PMID- 11074478
OWN - NLM
STAT- MEDLINE
DCOM- 20010125
LR  - 20191210
IS  - 0146-6615 (Print)
IS  - 0146-6615 (Linking)
VI  - 62
IP  - 4
DP  - 2000 Dec
TI  - Early interactions of human herpesvirus 6 with lymphoid cells: role of membrane 
      protein components and glycosaminoglycans in virus binding.
PG  - 487-97
AB  - A microassay was developed to detect human herpesvirus 6 (HHV-6) binding to its 
      cellular receptor using flow cytometry. Comparable results were obtained either 
      by using HHV-6 preparations conjugated with fluorescein isothiocyanate or by 
      indirect immunofluorescent labeling of membrane-bound virus using as primary 
      antibody a monoclonal antibody specific for the HHV-6 gp60/110 envelope 
      glycoprotein. Virus attachment to the plasma membrane was specific and saturable. 
      As expected, among cell lines of various origin, maximum binding was detected on 
      human T-lymphoid cells (HSB-2). Papain digestion of HSB-2 cells prevented HHV-6 
      attachment and reduced significantly virus infection, indicating the involvement 
      of a protein-based receptor in the attachment step. After removal of the 
      protease, virus receptors were resynthesized and their regeneration was prevented 
      partially by cycloheximide, an inhibitor of protein synthesis. Unexpectedly, only 
      high concentrations (mg/ml) of soluble heparan sulfate and heparin inhibited 
      HHV-6 binding and infection. Under the same conditions, few micrograms (per ml) 
      of heparin suppressed completely herpes simplex type 1 (HSV-1) attachment to the 
      same cell line. Treatment of HSB-2 cells with heparitinase and heparinase, at 
      doses that reduced significantly HSV-1 attachment, had little effect on HHV-6 
      binding to the cell membrane, indicating a different requirement of heparan 
      sulfate-containing glycosaminoglycans for the two herpesviruses. These data 
      suggest that protein components of the cellular membrane play an essential role 
      in HHV-6 binding and infection while heparan sulfate-glycos-aminoglycans appear 
      to be involved only partially in virus-receptor interaction.
CI  - Copyright 2000 Wiley-Liss, Inc.
FAU - Conti, C
AU  - Conti C
AD  - Istituto di Microbiologia, Universita di Roma "La Sapienza," Roma, Italy.
FAU - Cirone, M
AU  - Cirone M
FAU - Sgro, R
AU  - Sgro R
FAU - Altieri, F
AU  - Altieri F
FAU - Zompetta, C
AU  - Zompetta C
FAU - Faggioni, A
AU  - Faggioni A
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Med Virol
JT  - Journal of medical virology
JID - 7705876
RN  - 0 (Carbohydrates)
RN  - 0 (Enzymes)
RN  - 0 (Glycosaminoglycans)
RN  - 0 (Membrane Proteins)
RN  - 0 (Receptors, Virus)
SB  - IM
MH  - Animals
MH  - Carbohydrate Metabolism
MH  - Carbohydrates/physiology
MH  - Cell Line
MH  - Chlorocebus aethiops
MH  - Enzymes/metabolism
MH  - Flow Cytometry/methods
MH  - Glycosaminoglycans/metabolism/*physiology
MH  - Herpesvirus 6, Human/*metabolism
MH  - Humans
MH  - Lymphocytes/metabolism/*virology
MH  - Membrane Proteins/metabolism/*physiology
MH  - Receptors, Virus/biosynthesis/metabolism/*physiology
MH  - Time Factors
MH  - Tumor Cells, Cultured
MH  - Vero Cells
EDAT- 2000/11/14 11:00
MHDA- 2001/02/28 10:01
CRDT- 2000/11/14 11:00
PHST- 2000/11/14 11:00 [pubmed]
PHST- 2001/02/28 10:01 [medline]
PHST- 2000/11/14 11:00 [entrez]
AID - 10.1002/1096-9071(200012)62:4<487::AID-JMV14>3.0.CO;2-I [pii]
AID - 10.1002/1096-9071(200012)62:4<487::aid-jmv14>3.0.co;2-i [doi]
PST - ppublish
SO  - J Med Virol. 2000 Dec;62(4):487-97. doi: 
      10.1002/1096-9071(200012)62:4<487::aid-jmv14>3.0.co;2-i.