PMID- 12502850
OWN - NLM
STAT- MEDLINE
DCOM- 20030122
LR  - 20190508
IS  - 0022-538X (Print)
IS  - 1098-5514 (Electronic)
IS  - 0022-538X (Linking)
VI  - 77
IP  - 2
DP  - 2003 Jan
TI  - Differential N-linked glycosylation of human immunodeficiency virus and Ebola 
      virus envelope glycoproteins modulates interactions with DC-SIGN and DC-SIGNR.
PG  - 1337-46
AB  - The C-type lectins DC-SIGN and DC-SIGNR [collectively referred to as DC-SIGN(R)] 
      bind and transmit human immunodeficiency virus (HIV) and simian immunodeficiency 
      virus to T cells via the viral envelope glycoprotein (Env). Other viruses 
      containing heavily glycosylated glycoproteins (GPs) fail to interact with 
      DC-SIGN(R), suggesting some degree of specificity in this interaction. We show 
      here that DC-SIGN(R) selectively interact with HIV Env and Ebola virus GPs 
      containing more high-mannose than complex carbohydrate structures. Modulation of 
      N-glycans on Env or GP through production of viruses in different primary cells 
      or in the presence of the mannosidase I inhibitor deoxymannojirimycin 
      dramatically affected DC-SIGN(R) infectivity enhancement. Further, murine 
      leukemia virus, which typically does not interact efficiently with DC-SIGN(R), 
      could do so when produced in the presence of deoxymannojirimycin. We predict that 
      other viruses containing GPs with a large proportion of high-mannose N-glycans 
      will efficiently interact with DC-SIGN(R), whereas those with solely complex 
      N-glycans will not. Thus, the virus-producing cell type is an important factor in 
      dictating both N-glycan status and virus interactions with DC-SIGN(R), which may 
      impact virus tropism and transmissibility in vivo.
FAU - Lin, George
AU  - Lin G
AD  - Hematology-Oncology Division, Department of Medicine, University of Pennsylvania, 
      Philadelphia 19104, USA.
FAU - Simmons, Graham
AU  - Simmons G
FAU - Pohlmann, Stefan
AU  - Pohlmann S
FAU - Baribaud, Frederic
AU  - Baribaud F
FAU - Ni, Houping
AU  - Ni H
FAU - Leslie, George J
AU  - Leslie GJ
FAU - Haggarty, Beth S
AU  - Haggarty BS
FAU - Bates, Paul
AU  - Bates P
FAU - Weissman, Drew
AU  - Weissman D
FAU - Hoxie, James A
AU  - Hoxie JA
FAU - Doms, Robert W
AU  - Doms RW
LA  - eng
GR  - R01 35383/PHS HHS/United States
GR  - R01 AI43455/AI/NIAID NIH HHS/United States
GR  - R01 AI045378/AI/NIAID NIH HHS/United States
GR  - R01 AI043455/AI/NIAID NIH HHS/United States
GR  - HL62060-04/HL/NHLBI NIH HHS/United States
GR  - P30 AI45008/AI/NIAID NIH HHS/United States
GR  - P30 AI045008/AI/NIAID NIH HHS/United States
GR  - CA76256/CA/NCI NIH HHS/United States
GR  - R01 CA076256/CA/NCI NIH HHS/United States
GR  - R01 40880/PHS HHS/United States
GR  - R01 AI45378/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 (CLEC4M protein, human)
RN  - 0 (Cell Adhesion Molecules)
RN  - 0 (DC-specific ICAM-3 grabbing nonintegrin)
RN  - 0 (Lectins, C-Type)
RN  - 0 (Polysaccharides)
RN  - 0 (Receptors, Cell Surface)
RN  - 0 (Viral Envelope Proteins)
SB  - IM
MH  - Cell Adhesion Molecules/*metabolism
MH  - Cell Line
MH  - Ebolavirus/*metabolism
MH  - Glycosylation
MH  - HIV/*metabolism
MH  - Humans
MH  - Lectins, C-Type/*metabolism
MH  - Polysaccharides/metabolism
MH  - Receptors, Cell Surface/*metabolism
MH  - Viral Envelope Proteins/chemistry/*metabolism
PMC - PMC140807
EDAT- 2002/12/28 04:00
MHDA- 2003/01/23 04:00
PMCR- 2003/01/01
CRDT- 2002/12/28 04:00
PHST- 2002/12/28 04:00 [pubmed]
PHST- 2003/01/23 04:00 [medline]
PHST- 2002/12/28 04:00 [entrez]
PHST- 2003/01/01 00:00 [pmc-release]
AID - 1355 [pii]
AID - 10.1128/jvi.77.2.1337-1346.2003 [doi]
PST - ppublish
SO  - J Virol. 2003 Jan;77(2):1337-46. doi: 10.1128/jvi.77.2.1337-1346.2003.