DC-SIGN Interactions with Human Immunodeficiency Virus: Virus Binding and Transfer Are Dissociable Functions

Pöhlmann, Stefan; Leslie, George J.; Edwards, Terri G.; Macfarlan, Todd S.; Reeves, Jacqueline D.; Hiebenthal-Millow, Kirsten; Kirchhoff, Frank; Baribaud, Frédéric; Doms, Robert W.

doi:10.1128/jvi.75.21.10523-10526.2001

Cited by 65 publications

(53 citation statements)

References 13 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Studies using HEK293T cells transiently expressing DC-SIGN and L-SIGN have suggested that both CLRs are able to bind and transmit HIV-1 (9,47). Although 293T CLR transfectants can capture and transmit virus better than control transfectants, we have observed that HIV-1 transmission by 293T cells expressing high levels of DC-SIGN is significantly less efficient than by Raji/DC-SIGN cells or primary DCs (data not shown).…”

Section: Hiv-1 Transmission (46) Recent Studies Have Also Shown Thatmentioning

confidence: 57%

HIV-1 Transmission by Dendritic Cell-specific ICAM-3-grabbing Nonintegrin (DC-SIGN) Is Regulated by Determinants in the Carbohydrate Recognition Domain That Are Absent in Liver/Lymph Node-SIGN (L-SIGN)

Chung

Breun

Bashirova

et al. 2010

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

Section: Hiv-1 Transmission (46) Recent Studies Have Also Shown Thatmentioning

confidence: 57%

HIV-1 Transmission by Dendritic Cell-specific ICAM-3-grabbing Nonintegrin (DC-SIGN) Is Regulated by Determinants in the Carbohydrate Recognition Domain That Are Absent in Liver/Lymph Node-SIGN (L-SIGN)

Chung

Breun

Bashirova

et al. 2010

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…Whether the poor virus transmission is caused by a weak interaction between the viral envelope and CD209L2 remains to be determined. However, virus binding and transmission by CD209 are dissociable functions (19), and it is possible that the structural differences between CD209 and CD209L2 specifically affect the process of virus transmission by CD209L2 while maintaining strong binding of the virus. Further investigation of the mechanistic basis of the poor transmission of HIV-1 or SIV by CD209L2 should involve detailed analysis of both virus binding and transmission by using various chimeric and mutant constructs.…”

Section: Discussionmentioning

confidence: 99%

Novel Member of the CD209 ( DC-SIGN ) Gene Family in Primates

Bashirova

Cheng

et al. 2003

J Virol

View full text Add to dashboard Cite

Two CD209 family genes identified in humans, CD209 (DC-SIGN) and CD209L (DC-SIGNR/L-SIGN), encode C-type lectins that serve as adhesion receptors for ICAM-2 and ICAM-3 and participate in the transmission of human and simian immunodeficiency viruses (HIV and SIV, respectively) to target cells in vitro. Here we characterize the CD209 gene family in nonhuman primates and show that recent evolutionary alterations have occurred in this family across primate species. All of the primate species tested, specifically, Old World monkeys (OWM) and apes, have orthologues of human CD209. In contrast, CD209L is missing in OWM but present in apes. A third family member, that we have named CD209L2, was cloned from rhesus monkey cDNA and subsequently identified in OWM and apes but not in humans. Rhesus CD209L2 mRNA was prominently expressed in the liver and axillary lymph nodes, although preliminary data suggest that levels of expression may vary among individuals. Despite a high level of sequence similarity to both human and rhesus CD209, rhesus CD209L2 was substantially less effective at binding ICAM-3 and poorly transmitted HIV type 1 and SIV to target cells relative to CD209. Our data suggest that the CD209 gene family has undergone recent evolutionary processes involving duplications and deletions, the latter of which may be tolerated because of potentially redundant functional activities of the molecules encoded by these genes.

show abstract

“…A stop codon at the gp120-gp41 cleavage site was generated by QuikChange (Stratagene). Plasmids expressing CD4, CXCR4, CCR5, and CCR5/N13D (25,35); DC-SIGN, DC-SIGNR, rhesus DC-SIGN, pigtailed DC-SIGN, and murine DC-SIGN (3,(43)(44)(45); EboZ-GP and EboS-GP (50); and vesicular stomatitis virus G (VSV-G) and amphotropic murine leukemia virus (MLV) Env (pHit 456) have been described (50a). The ASGP-R1 subunit of the hepatic ASGP-R was PCR amplified from a human liver cDNA library (Clontech) and was subcloned into pcDNA6-B (Invitrogen) by using NheI and SaeII to give a C-terminal V5/His tag.…”

Section: Methodsmentioning

confidence: 99%

Differential N-Linked Glycosylation of Human Immunodeficiency Virus and Ebola Virus Envelope Glycoproteins Modulates Interactions with DC-SIGN and DC-SIGNR

Lin

Simmons²,

Pöhlmann³

et al. 2003

J Virol

Self Cite

247

220

View full text Add to dashboard Cite

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.

show abstract

DC-SIGN Interactions with Human Immunodeficiency Virus: Virus Binding and Transfer Are Dissociable Functions

Cited by 65 publications

References 13 publications

HIV-1 Transmission by Dendritic Cell-specific ICAM-3-grabbing Nonintegrin (DC-SIGN) Is Regulated by Determinants in the Carbohydrate Recognition Domain That Are Absent in Liver/Lymph Node-SIGN (L-SIGN)

HIV-1 Transmission by Dendritic Cell-specific ICAM-3-grabbing Nonintegrin (DC-SIGN) Is Regulated by Determinants in the Carbohydrate Recognition Domain That Are Absent in Liver/Lymph Node-SIGN (L-SIGN)

Novel Member of the CD209 ( DC-SIGN ) Gene Family in Primates

Differential N-Linked Glycosylation of Human Immunodeficiency Virus and Ebola Virus Envelope Glycoproteins Modulates Interactions with DC-SIGN and DC-SIGNR

Contact Info

Product

Resources

About