This title appears in the Scientific Report :
2006
Please use the identifier:
http://dx.doi.org/10.1074/jbcM505012200 in citations.
Please use the identifier: http://hdl.handle.net/2128/2646 in citations.
Glutamic acid-rich proteins of rod photoreceptors are natively unfolded
Glutamic acid-rich proteins of rod photoreceptors are natively unfolded
Broadly neutralizing HIV antibodies (bNAbs) can recognize carbohydrate-dependent epitopes on gp120. In contrast to previously characterized glycan-dependent bNAbs that recognize high-mannose N-glycans, PGT121 binds complex-type N-glycans in glycan microarrays. We isolated the B-cell clone encoding P...
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Personal Name(s): | Batra-Safferling, R. |
---|---|
Abarca-Heidemann, K. / Körschen, H. G. / Tziatzios, C. / Stoldt, M. / Budyak, I. / Willbold, D. / Schwalbe, H. / Klein-Seetharaman, J. / Kaupp, U. B. | |
Contributing Institute: |
Zelluläre Signalverarbeitung; IBI-1 Biologische Strukturforschung; IBI-2 |
Published in: | The @journal of biological chemistry, 281 (2006) S. 1449 - 1460 |
Imprint: |
Bethesda, Md.
Soc.
2006
|
Physical Description: |
1449 - 1460 |
PubMed ID: |
23115339 |
DOI: |
10.1074/jbcM505012200 |
Document Type: |
Journal Article |
Research Program: |
Funktion und Dysfunktion des Nervensystems |
Series Title: |
Journal of Biological Chemistry
281 |
Subject (ZB): | |
Link: |
Get full text OpenAccess |
Publikationsportal JuSER |
Please use the identifier: http://hdl.handle.net/2128/2646 in citations.
Broadly neutralizing HIV antibodies (bNAbs) can recognize carbohydrate-dependent epitopes on gp120. In contrast to previously characterized glycan-dependent bNAbs that recognize high-mannose N-glycans, PGT121 binds complex-type N-glycans in glycan microarrays. We isolated the B-cell clone encoding PGT121, which segregates into PGT121-like and 10-1074-like groups distinguished by sequence, binding affinity, carbohydrate recognition, and neutralizing activity. Group 10-1074 exhibits remarkable potency and breadth but no detectable binding to protein-free glycans. Crystal structures of unliganded PGT121, 10-1074, and their likely germ-line precursor reveal that differential carbohydrate recognition maps to a cleft between complementarity determining region (CDR)H2 and CDRH3. This cleft was occupied by a complex-type N-glycan in a "liganded" PGT121 structure. Swapping glycan contact residues between PGT121 and 10-1074 confirmed their importance for neutralization. Although PGT121 binds complex-type N-glycans, PGT121 recognized high-mannose-only HIV envelopes in isolation and on virions. As HIV envelopes exhibit varying proportions of high-mannose- and complex-type N-glycans, these results suggest promiscuous carbohydrate interactions, an advantageous adaptation ensuring neutralization of all viruses within a given strain. |