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, Nancy P. Y.; Breun, Sabine; Bashirova, Arman; Baumann, Joerg G.; Martin, Thomas; Karamchandani, Jaideep M.; Rausch, Jason W.; Grice, Stuart F. J. Le; Wu, Li; Carrington, Mary; KewalRamani, Vineet N.

doi:10.1074/jbc.m109.030619

Cited by 26 publications

(38 citation statements)

References 51 publications

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“…[6] Despite sharing 77 %a mino acid identity and an overall tetrameric structure,D C-SIGN/R have shown to possess notable differences in glycan binding affinity,s pecificity and viral transmission efficiency. Fore xample,D C-SIGN recognizes and transmits some HIV strains more effectively than DC-SIGNR, [7] whereas only DC-SIGNR promotes West Nile Virus (WNV) infection with high efficiency. [8] Given individual CRD-mannose binding motifs are identical in DC-SIGN/ R [5b] and the binding affinities are very weak (K D % mm), [9] such differences must stem from their different multivalent binding properties which are still poorly understood.…”

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confidence: 99%

Compact, Polyvalent Mannose Quantum Dots as Sensitive, Ratiometric FRET Probes for Multivalent Protein–Ligand Interactions

et al. 2016

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A highly efficient cap‐exchange approach for preparing compact, dense polyvalent mannose‐capped quantum dots (QDs) has been developed. The resulting QDs have been successfully used to probe multivalent interactions of HIV/Ebola receptors DC‐SIGN and DC‐SIGNR (collectively termed as DC‐SIGN/R) using a sensitive, ratiometric Förster resonance energy transfer (FRET) assay. The QD probes specifically bind DC‐SIGN, but not its closely related receptor DC‐SIGNR, which is further confirmed by its specific blocking of DC‐SIGN engagement with the Ebola virus glycoprotein. Tuning the QD surface mannose valency reveals that DC‐SIGN binds more efficiently to densely packed mannosides. A FRET‐based thermodynamic study reveals that the binding is enthalpy‐driven. This work establishes QD FRET as a rapid, sensitive technique for probing structure and thermodynamics of multivalent protein–ligand interactions.

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confidence: 99%

Compact, Polyvalent Mannose Quantum Dots as Sensitive, Ratiometric FRET Probes for Multivalent Protein–Ligand Interactions

et al. 2016

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“…The latter, while they remain non-productively infected, can mediate the infection of T cells [21]. Simillarly, DCs that have captured HIV-1 through their sugar binding receptors [22] can transfer the virus through viral synapses [23], to remote CD4 T cells [24]–[26]. Nevertheless, a direct evidence for the implication of mucosal dendritic cells in the transmission of HIV-1 in vivo is still lacking.…”

Section: Discussionmentioning

confidence: 99%

HIV-1 Expressing the Envelopes of Transmitted/Founder or Control/Reference Viruses Have Similar Infection Patterns of CD4 T-Cells in Human Cervical Tissue Ex Vivo

et al. 2012

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Recently, it was found that 80% of sexual HIV-1 transmissions are established by a single virion/viral genome. To investigate whether the transmitted/founder (T/F) viruses have specific biological properties favoring sexual transmission, we inoculated human cervical tissue explants with isogenic HIV-1 viruses encoding Env sequences from T/F and control reference (C/R) HIV-1 variants as well as with full length T/F HIV-1 and compared their replication efficiencies, T cell depletion, and the activation status of infected cells. We found that all the HIV-1 variants were capable of transmitting infection to cervical tissue ex vivo and in this system preferentially replicate in activated CD4 T cells and deplete these cells. There was no difference in the biological properties of T/F and C/R HIV-1 variants as evaluated in ex vivo cervical tissue.

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“…The HIV-1 proviral DNA construct pNL4 -3 (16) and the expression plasmid for an HIV-1 Gag-GFP fusion protein (42) were gifts from Dr. Vineet KewalRamani and Dr. Alan Rein (National Cancer Institute), respectively. The HIV-1 Env expression constructs pIIINL4env and pAD8 Env were gifts from Dr. Eric Freed (National Cancer Institute).…”

Section: Plasmids and Recombinant Proteinsmentioning

confidence: 99%

HIV-1 envelope proteins up-regulate N6-methyladenosine levels of cellular RNA independently of viral replication

Tirumuru

2019

Journal of Biological Chemistry

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Edited by Charles E. Samuel N 6 -methyladenosine (m 6 A) modification of HIV-1 RNA regulates viral replication and protein expression. The m 6 A modification is regulated by two groups of cellular proteins named writers and erasers that add or remove m 6 A, respectively. HIV-1 infection of CD4 ؉ T-cells increases m 6 A levels of cellular mRNA, but the underlying mechanism is unknown. Here, we show that HIV-1 infection of CD4 ؉ primary T-cells or Jurkat cells significantly increases m 6 A levels of cellular RNA independently of viral replication. Compared with HIV-1-infected CD4 ؉ T-cells, similar m 6 A up-regulation was detected in total RNA from HIV-1-infected cells treated with a reverse-transcriptase inhibitor or with heat-inactivated HIV-1. Compared with mock controls, significantly increased m 6 A levels were detected in total RNA from Jurkat cells infected by single-cycle HIV-1 pseudotyped with an HIV-1 envelope (Env) glycoprotein, but not with vesicular stomatitis virus glycoprotein G (VSV-G).Overexpression of HIV-1 Env in HEK293T cells did not affect m 6 A levels of cellular RNA, suggesting that de novo synthesis of Env is not required for m 6 A up-regulation. Interestingly, treatment of Jurkat cells with recombinant gp120 of HIV-1 Env significantly increased m 6 A levels of cellular RNA, which was reduced by a gp120-neutralizing antibody. Preincubation of Jurkat cells with a CD4 receptor-neutralizing antibody blocked HIV-1-induced up-regulation of m 6 A levels in cellular RNA. Moreover, HIV-1 infection or gp120 treatment did not alter the protein expression of m 6 A writers and erasers in cells. Our findings suggest that HIV-1 gp120 binding to the CD4 receptor is required for m 6 A up-regulation in cells. . 2 The abbreviations used are: m 6 A, N 6 -methyladenosine; MOI, multiplicity of infection; hpi, hours post-infection; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; NVP, nevirapine; Env, HIV-1 envelope proteins; METTL, methyltransferase-like protein; FTO, fat mass and obesity-associated protein; AlkBH5, AlkB family member 5; MB, methylene blue; sncRNA, small noncoding RNA; sCD4, soluble CD4; NARP, National Institutes of Health AIDS Reagent Program; SSC, saline-sodium citrate.

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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)

Abstract: In this study, we identify determinants in dendritic cell

Cited by 26 publications

References 51 publications

Compact, Polyvalent Mannose Quantum Dots as Sensitive, Ratiometric FRET Probes for Multivalent Protein–Ligand Interactions

Compact, Polyvalent Mannose Quantum Dots as Sensitive, Ratiometric FRET Probes for Multivalent Protein–Ligand Interactions

HIV-1 Expressing the Envelopes of Transmitted/Founder or Control/Reference Viruses Have Similar Infection Patterns of CD4 T-Cells in Human Cervical Tissue Ex Vivo

HIV-1 envelope proteins up-regulate N6-methyladenosine levels of cellular RNA independently of viral replication

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