ArticlePloS one2010
Crystal structure of the neutralizing Llama V(HH) D7 and its mode of HIV-1 gp120 interaction.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
19 citing papers in PubMed, 37 citations in OpenAlex.
- Nanobodies in the fight against infectious diseases: repurposing nature's tiny weapons.World journal of microbiology & biotechnology · 2024Review
- Structural basis for llama nanobody recognition and neutralization of HIV-1 at the CD4-binding site.Structure (London, England : 1993) · 2022Article
- VInternational journal of molecular sciences · 2022Review
- Nanobodies that Neutralize HIV.Vaccines · 2019Review
- Super Potent Bispecific Llama VHH Antibodies Neutralize HIV via a Combination of gp41 and gp120 Epitopes.Antibodies (Basel, Switzerland) · 2019Article
- Nanobodies targeting norovirus capsid reveal functional epitopes and potential mechanisms of neutralization.PLoS pathogens · 2017Article
- Unveiling a Drift Resistant Cryptotope withinFrontiers in immunology · 2017Article
- Nanobody-derived nanobiotechnology tool kits for diverse biomedical and biotechnology applications.International journal of nanomedicine · 2016Review
- Nanobody binding to a conserved epitope promotes norovirus particle disassembly.Journal of virology · 2015Article
- Article
- Structural basis for the inhibition of HIV-1 Nef by a high-affinity binding single-domain antibody.Retrovirology · 2014Article
- Preventive and therapeutic applications of neutralizing antibodies to Human Immunodeficiency Virus Type 1 (HIV-1).Therapeutic advances in vaccines · 2013Article
- A gp41 MPER-specific llama VHH requires a hydrophobic CDR3 for neutralization but not for antigen recognition.PLoS pathogens · 2013Article
- Potent and broad neutralization of HIV-1 by a llama antibody elicited by immunization.The Journal of experimental medicine · 2012Article
- MiniCD4 protein resistance mutations affect binding to the HIV-1 gp120 CD4 binding site and decrease entry efficiency.Retrovirology · 2012Article
- Llama antibody fragments recognizing various epitopes of the CD4bs neutralize a broad range of HIV-1 subtypes A, B and C.PloS one · 2012Article
- Future opportunities for passive immunity against viral diseases.The Journal of infectious diseases · 2011Article
- Biotechnological applications of recombinant single-domain antibody fragments.Microbial cell factories · 2011Review
- Generation of a family-specific phage library of llama single chain antibody fragments that neutralize HIV-1.The Journal of biological chemistry · 2010Article
Corrections and comments
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Authors and funding
10 authors at 5 institutions in 3 countries.
Funding
Abstract
HIV-1 entry into host cells is mediated by the sequential binding of the envelope glycoprotein gp120 to CD4 and a chemokine receptor. Antibodies binding to epitopes overlapping the CD4-binding site on gp120 are potent inhibitors of HIV entry, such as the llama heavy chain antibody fragment V(HH) D7, which has cross-clade neutralizing properties and competes with CD4 and mAb b12 for high affinity binding to gp120. We report the crystal structure of the D7 V(HH) at 1.5 A resolution, which reveals the molecular details of the complementarity determining regions (CDR) and substantial flexibility of CDR3 that could facilitate an induced fit interaction with gp120. Structural comparison of CDRs from other CD4 binding site antibodies suggests diverse modes of interaction. Mutational analysis identified CDR3 as a key component of gp120 interaction as determined by surface plasmon resonance. A decrease in affinity is directly coupled to the neutralization efficiency since mutations that decrease gp120 interaction increase the IC50 required for HIV-1 IIIB neutralization. Thus the structural study identifies the long CDR3 of D7 as the key determinant of interaction and HIV-1 neutralization. Furthermore, our data confirm that the structural plasticity of gp120 can accommodate multiple modes of antibody binding within the CD4 binding site.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.