Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Publication Date: 2011-10-15
    Description: The HIV envelope (Env) protein gp120 is protected from antibody recognition by a dense glycan shield. However, several of the recently identified PGT broadly neutralizing antibodies appear to interact directly with the HIV glycan coat. Crystal structures of antigen-binding fragments (Fabs) PGT 127 and 128 with Man(9) at 1.65 and 1.29 angstrom resolution, respectively, and glycan binding data delineate a specific high mannose-binding site. Fab PGT 128 complexed with a fully glycosylated gp120 outer domain at 3.25 angstroms reveals that the antibody penetrates the glycan shield and recognizes two conserved glycans as well as a short beta-strand segment of the gp120 V3 loop, accounting for its high binding affinity and broad specificity. Furthermore, our data suggest that the high neutralization potency of PGT 127 and 128 immunoglobulin Gs may be mediated by cross-linking Env trimers on the viral surface.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3280215/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3280215/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pejchal, Robert -- Doores, Katie J -- Walker, Laura M -- Khayat, Reza -- Huang, Po-Ssu -- Wang, Sheng-Kai -- Stanfield, Robyn L -- Julien, Jean-Philippe -- Ramos, Alejandra -- Crispin, Max -- Depetris, Rafael -- Katpally, Umesh -- Marozsan, Andre -- Cupo, Albert -- Maloveste, Sebastien -- Liu, Yan -- McBride, Ryan -- Ito, Yukishige -- Sanders, Rogier W -- Ogohara, Cassandra -- Paulson, James C -- Feizi, Ten -- Scanlan, Christopher N -- Wong, Chi-Huey -- Moore, John P -- Olson, William C -- Ward, Andrew B -- Poignard, Pascal -- Schief, William R -- Burton, Dennis R -- Wilson, Ian A -- AI082362/AI/NIAID NIH HHS/ -- AI33292/AI/NIAID NIH HHS/ -- AI74372/AI/NIAID NIH HHS/ -- AI84817/AI/NIAID NIH HHS/ -- F32 AI074372-03/AI/NIAID NIH HHS/ -- HFE-224662/Canadian Institutes of Health Research/Canada -- P01 AI082362/AI/NIAID NIH HHS/ -- P01 AI082362-03/AI/NIAID NIH HHS/ -- P01 AI082362-04/AI/NIAID NIH HHS/ -- P41RR001209/RR/NCRR NIH HHS/ -- R01 AI033292/AI/NIAID NIH HHS/ -- R01 AI033292-14/AI/NIAID NIH HHS/ -- R01 AI084817/AI/NIAID NIH HHS/ -- R01 AI084817-04/AI/NIAID NIH HHS/ -- RR017573/RR/NCRR NIH HHS/ -- U01 CA128416/CA/NCI NIH HHS/ -- Y1-CO-1020/CO/NCI NIH HHS/ -- Y1-GM-1104/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2011 Nov 25;334(6059):1097-103. doi: 10.1126/science.1213256. Epub 2011 Oct 13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Skaggs Institute for Chemical Biology and International AIDS Vaccine Initiative (IAVI) Neutralizing Antibody Center, nhe Scripps Research Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21998254" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Neutralizing/chemistry/genetics/*immunology/metabolism ; Antibody Specificity ; Binding Sites, Antibody ; Carbohydrate Conformation ; Cell Line ; Crystallography, X-Ray ; Disaccharides/chemistry/metabolism ; Epitopes ; Glycosylation ; HIV Antibodies/chemistry/genetics/*immunology/*metabolism ; HIV Envelope Protein gp120/chemistry/*immunology/metabolism ; HIV-1/*immunology/physiology ; Humans ; Hydrogen Bonding ; Immunoglobulin Fab Fragments/chemistry/immunology/metabolism ; Mannose/chemistry/immunology/metabolism ; Mannosides/chemistry/metabolism ; Models, Molecular ; Mutation ; Oligosaccharides/chemistry/*immunology/metabolism ; Polysaccharides/chemistry/*immunology/*metabolism ; Protein Conformation ; Protein Structure, Tertiary
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Signatur Availability
    BibTip Others were also interested in ...
  • 2
    Publication Date: 2012-07-17
    Description: Certain human pathogens avoid elimination by our immune system by rapidly mutating the surface protein sites targeted by antibody responses, and consequently they tend to be problematic for vaccine development. The behavior described is prominent for a subset of viruses--the highly antigenically diverse viruses--which include HIV, influenza, and hepatitis C viruses. However, these viruses do harbor highly conserved exposed sites, usually associated with function, which can be targeted by broadly neutralizing antibodies. Until recently, not many such antibodies were known, but advances in the field have enabled increasing numbers to be identified. Molecular characterizations of the antibodies and, most importantly, of the sites of vulnerability that they recognize give hope for the discovery of new vaccines and drugs.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3600854/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3600854/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Burton, Dennis R -- Poignard, Pascal -- Stanfield, Robyn L -- Wilson, Ian A -- P01 AI082362/AI/NIAID NIH HHS/ -- R01 AI084817/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2012 Jul 13;337(6091):183-6. doi: 10.1126/science.1225416.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology and Microbial Science and International AIDS Vaccine Initiative Neutralizing Antibody Center, The Scripps Research Institute, La Jolla, CA 92037, USA. burton@scripps.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22798606" target="_blank"〉PubMed〈/a〉
    Keywords: AIDS Vaccines/immunology ; Animals ; Antibodies, Neutralizing/*immunology ; Antibodies, Viral/*immunology ; *Antigenic Variation ; Drug Discovery ; HIV Antibodies/chemistry/*immunology ; HIV Infections/immunology/prevention & control ; HIV-1/*immunology/pathogenicity ; Hepacivirus/*immunology ; Hepatitis C/immunology/prevention & control ; Humans ; Influenza Vaccines ; Influenza, Human/immunology/prevention & control ; Models, Molecular ; Orthomyxoviridae/*immunology ; env Gene Products, Human Immunodeficiency Virus/chemistry/immunology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Signatur Availability
    BibTip Others were also interested in ...
  • 3
    Publication Date: 2013-11-02
    Description: HIV-1 entry into CD4(+) target cells is mediated by cleaved envelope glycoprotein (Env) trimers that have been challenging to characterize structurally. Here, we describe the crystal structure at 4.7 angstroms of a soluble, cleaved Env trimer that is stabilized and antigenically near-native (termed the BG505 SOSIP.664 gp140 trimer) in complex with a potent broadly neutralizing antibody, PGT122. The structure shows a prefusion state of gp41, the interaction between the component gp120 and gp41 subunits, and how a close association between the gp120 V1/V2/V3 loops stabilizes the trimer apex around the threefold axis. The complete epitope of PGT122 on the trimer involves gp120 V1, V3, and several surrounding glycans. This trimer structure advances our understanding of how Env functions and is presented to the immune system, and provides a blueprint for structure-based vaccine design.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3886632/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3886632/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Julien, Jean-Philippe -- Cupo, Albert -- Sok, Devin -- Stanfield, Robyn L -- Lyumkis, Dmitry -- Deller, Marc C -- Klasse, Per-Johan -- Burton, Dennis R -- Sanders, Rogier W -- Moore, John P -- Ward, Andrew B -- Wilson, Ian A -- GM103310/GM/NIGMS NIH HHS/ -- P01 AI082362/AI/NIAID NIH HHS/ -- P01 AI82362/AI/NIAID NIH HHS/ -- P41 GM103310/GM/NIGMS NIH HHS/ -- P41RR001209/RR/NCRR NIH HHS/ -- R01 AI033292/AI/NIAID NIH HHS/ -- R01 AI084817/AI/NIAID NIH HHS/ -- R01 AI33292/AI/NIAID NIH HHS/ -- R37 AI036082/AI/NIAID NIH HHS/ -- R37 AI36082/AI/NIAID NIH HHS/ -- U54 GM094586/GM/NIGMS NIH HHS/ -- UM1 AI100663/AI/NIAID NIH HHS/ -- Y1-CO-1020/CO/NCI NIH HHS/ -- Y1-GM-1104/GM/NIGMS NIH HHS/ -- Canadian Institutes of Health Research/Canada -- New York, N.Y. -- Science. 2013 Dec 20;342(6165):1477-83. doi: 10.1126/science.1245625. Epub 2013 Oct 31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24179159" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Neutralizing/chemistry ; Antibodies, Viral/chemistry ; Crystallography, X-Ray ; HIV Envelope Protein gp120/chemistry/immunology ; HIV Envelope Protein gp41/chemistry/immunology ; Humans ; Protein Multimerization ; Protein Structure, Quaternary ; Recombinant Proteins/chemistry/immunology ; Solubility ; env Gene Products, Human Immunodeficiency Virus/*chemistry/immunology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Signatur Availability
    BibTip Others were also interested in ...
  • 4
    Publication Date: 2013-11-30
    Description: Hepatitis C virus (HCV), a Hepacivirus, is a major cause of viral hepatitis, liver cirrhosis, and hepatocellular carcinoma. HCV envelope glycoproteins E1 and E2 mediate fusion and entry into host cells and are the primary targets of the humoral immune response. The crystal structure of the E2 core bound to broadly neutralizing antibody AR3C at 2.65 angstroms reveals a compact architecture composed of a central immunoglobulin-fold beta sandwich flanked by two additional protein layers. The CD81 receptor binding site was identified by electron microscopy and site-directed mutagenesis and overlaps with the AR3C epitope. The x-ray and electron microscopy E2 structures differ markedly from predictions of an extended, three-domain, class II fusion protein fold and therefore provide valuable information for HCV drug and vaccine design.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3954638/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3954638/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kong, Leopold -- Giang, Erick -- Nieusma, Travis -- Kadam, Rameshwar U -- Cogburn, Kristin E -- Hua, Yuanzi -- Dai, Xiaoping -- Stanfield, Robyn L -- Burton, Dennis R -- Ward, Andrew B -- Wilson, Ian A -- Law, Mansun -- AI071084/AI/NIAID NIH HHS/ -- AI079031/AI/NIAID NIH HHS/ -- AI080916/AI/NIAID NIH HHS/ -- AI084817/AI/NIAID NIH HHS/ -- P41 GM103310/GM/NIGMS NIH HHS/ -- P41RR001209/RR/NCRR NIH HHS/ -- R01 AI071084/AI/NIAID NIH HHS/ -- R01 AI079031/AI/NIAID NIH HHS/ -- R01 AI084817/AI/NIAID NIH HHS/ -- R21 AI080916/AI/NIAID NIH HHS/ -- RR017573/RR/NCRR NIH HHS/ -- U54 GM094586/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2013 Nov 29;342(6162):1090-4. doi: 10.1126/science.1243876.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24288331" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Neutralizing/chemistry ; Antigens, CD81/chemistry ; Antiviral Agents/chemistry ; Binding Sites ; Crystallography, X-Ray ; Drug Design ; Epitopes/chemistry/genetics ; Humans ; Immunoglobulin Fab Fragments/chemistry ; Mutagenesis, Site-Directed ; Protein Folding ; Protein Structure, Tertiary ; Viral Envelope Proteins/*chemistry/immunology ; Viral Hepatitis Vaccines/chemistry/immunology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Signatur Availability
    BibTip Others were also interested in ...
  • 5
    ISSN: 1600-5759
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Type of Medium: Electronic Resource
    Signatur Availability
    BibTip Others were also interested in ...
  • 6
    ISSN: 1520-4804
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    Signatur Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...