| Predicate |
Object |
| assignee |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_0c4322cb4de342be2dbedcbe0c278f6f
http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_a933a0dd561e3e50b278738704d5c6e6 |
| classificationCPCAdditional |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K2317-565
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K2317-76
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K2317-21 |
| classificationCPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/A61P31-18
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C07K16-1063
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/G01N33-56988
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/A61K39-42 |
| classificationIPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/A61P31-18
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-13
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/A61K39-42
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K16-10 |
| filingDate |
2012-03-23-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_de81a38a18c1385ea328ed64707ae228
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_c5a46b69371683ef6179fe1f36faba1d
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_b223a3ef37502e58abd861e0178bd00e
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_499224c8cf85e7372dcbdd8a1475bcf4
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_635906af621a127927ca0fe44363be2e
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_56ce4f0d98bf4660a969d42235c73022 |
| publicationDate |
2012-11-15-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber |
CA-2835522-A1 |
| titleOfInvention |
Focused evolution of hiv-1 neutralizing antibodies revealed by crystal structures and deep sequencing |
| abstract |
Antibody VRC01 represents a human immunoglobulin that neutralizes -~90% of diverse HIV-1 isolates. To understand how such broadly neutralizing HIV-1 antibodies develop and recognize the viral envelope, we used X-ray crystallography and 454 pyrosequencing to characterize additional antibodies from HIV-1-infected individuals. Crystal structures revealed a convergent mode of binding of different antibodies to the same CD4-binding-site epitope. Antibody recognition was achieved through the evolution of complementary contact domains that were generated in diverse ways. Phylogenetic analysis of expressed heavy and light chains determined by deep sequencing revealed a common pathway of antibody heavy chain maturation confined to IGHV1-2*02 lineage that could pair with different light chains. The maturation pathway inferred by antibodyomics reveals that diverse antibodies evolve to a highly affinity-matured state to recognize an invariant viral structure, providing insight into the development and evolution of broadly neutralizing HIV-1 immunity. |
| priorityDate |
2011-05-09-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type |
http://data.epo.org/linked-data/def/patent/Publication |