PMID- 11312337
OWN - NLM
STAT- MEDLINE
DCOM- 20010524
LR  - 20181113
IS  - 0022-538X (Print)
IS  - 1098-5514 (Electronic)
IS  - 0022-538X (Linking)
VI  - 75
IP  - 10
DP  - 2001 May
TI  - DC-SIGN interactions with human immunodeficiency virus type 1 and 2 and simian 
      immunodeficiency virus.
PG  - 4664-72
AB  - Dendritic cells (DCs) efficiently bind and transmit human immunodeficiency virus 
      (HIV) to cocultured T cells and so may play an important role in HIV 
      transmission. DC-SIGN, a novel C-type lectin that is expressed in DCs, has 
      recently been shown to bind R5 HIV type 1 (HIV-1) strains and a 
      laboratory-adapted X4 strain. To characterize the interaction of DC-SIGN with 
      primate lentiviruses, we investigated the structural determinants of DC-SIGN 
      required for virus binding and transmission to permissive cells. We constructed a 
      panel of DC-SIGN mutants and established conditions which allowed comparable cell 
      surface expression of all mutants. We found that R5, X4, and R5X4 HIV-1 isolates 
      as well as simian immunodeficiency and HIV-2 strains bound to DC-SIGN and could 
      be transmitted to CD4/coreceptor-positive cell types. DC-SIGN contains a single 
      N-linked carbohydrate chain that is important for efficient cell surface 
      expression but is not required for DC-SIGN-mediated virus binding and 
      transmission. In contrast, C-terminal deletions removing either the lectin 
      binding domain or the repeat region abrogated DC-SIGN function. Trypsin-EDTA 
      treatment inhibited DC-SIGN mediated infection, indicating that virus was 
      maintained at the surface of the DC-SIGN-expressing cells used in this study. 
      Finally, quantitative fluorescence-activated cell sorting analysis of AU1-tagged 
      DC-SIGN revealed that the efficiency of virus transmission was strongly affected 
      by variations in DC-SIGN expression levels. Thus, variations in DC-SIGN 
      expression levels on DCs could greatly affect the susceptibility of human 
      individuals to HIV infection.
FAU - Pohlmann, S
AU  - Pohlmann S
AD  - Department of Pathology and Laboratory Medicine, University of Pennsylvania, 
      Philadelphia, Pennsylvania 19104, USA.
FAU - Baribaud, F
AU  - Baribaud F
FAU - Lee, B
AU  - Lee B
FAU - Leslie, G J
AU  - Leslie GJ
FAU - Sanchez, M D
AU  - Sanchez MD
FAU - Hiebenthal-Millow, K
AU  - Hiebenthal-Millow K
FAU - Munch, J
AU  - Munch J
FAU - Kirchhoff, F
AU  - Kirchhoff F
FAU - Doms, R W
AU  - Doms RW
LA  - eng
GR  - P30 AI045008/AI/NIAID NIH HHS/United States
GR  - 40880/PHS HHS/United States
GR  - AI 35383/AI/NIAID NIH HHS/United States
GR  - P30-AI45008/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 (Cell Adhesion Molecules)
RN  - 0 (DC-specific ICAM-3 grabbing nonintegrin)
RN  - 0 (Lectins)
RN  - 0 (Lectins, C-Type)
RN  - 0 (Receptors, Cell Surface)
RN  - 0 (Receptors, Virus)
RN  - 9G34HU7RV0 (Edetic Acid)
RN  - EC 3.4.21.4 (Trypsin)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - *Cell Adhesion Molecules
MH  - Cell Line, Transformed
MH  - Cell Membrane/metabolism
MH  - Edetic Acid
MH  - Gene Expression
MH  - Glycosylation
MH  - HIV-1/*metabolism
MH  - HIV-2/*metabolism
MH  - Humans
MH  - Lectins/genetics/*metabolism
MH  - *Lectins, C-Type
MH  - Molecular Sequence Data
MH  - Mutagenesis
MH  - Receptors, Cell Surface/genetics/*metabolism
MH  - Receptors, Virus/genetics/*metabolism
MH  - Simian Immunodeficiency Virus/*metabolism
MH  - Trypsin
PMC - PMC114220
EDAT- 2001/04/20 10:00
MHDA- 2001/05/26 10:01
PMCR- 2001/05/01
CRDT- 2001/04/20 10:00
PHST- 2001/04/20 10:00 [pubmed]
PHST- 2001/05/26 10:01 [medline]
PHST- 2001/04/20 10:00 [entrez]
PHST- 2001/05/01 00:00 [pmc-release]
AID - 2280 [pii]
AID - 10.1128/JVI.75.10.4664-4672.2001 [doi]
PST - ppublish
SO  - J Virol. 2001 May;75(10):4664-72. doi: 10.1128/JVI.75.10.4664-4672.2001.