2013
DOI: 10.1126/science.1234914
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Structure of RSV Fusion Glycoprotein Trimer Bound to a Prefusion-Specific Neutralizing Antibody

Abstract: The respiratory syncytial virus (RSV) fusion (F) glycoprotein prefusion conformation is the target of most RSV-neutralizing activity in human sera, but its metastability has hindered characterization. To overcome this obstacle, we identified prefusion-specific antibodies which were substantially more potent than the prophylactic antibody palivizumab. The co-crystal structure for one of these antibodies, D25, in complex with the F glycoprotein revealed that D25 locks F in its prefusion state by binding to a qua… Show more

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Cited by 725 publications
(985 citation statements)
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“…It has been recently demonstrated that most of the neutralizing antibodies in human sera are directed against the prefusion form of hRSV F (Magro et al , 2012; Ngwuta et al , 2015) and that prefusion‐specific site Ø mAbs are the most potent neutralizing antibodies (McLellan et al , 2013b; McLellan, 2015). For this reason, and to test the possibility of extending the chimera approach to other conformations and antigenic sites, the chimeric proteins F‐410, F‐411, and F‐412 of Fig EV1 were produced.…”
Section: Resultsmentioning
confidence: 99%
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“…It has been recently demonstrated that most of the neutralizing antibodies in human sera are directed against the prefusion form of hRSV F (Magro et al , 2012; Ngwuta et al , 2015) and that prefusion‐specific site Ø mAbs are the most potent neutralizing antibodies (McLellan et al , 2013b; McLellan, 2015). For this reason, and to test the possibility of extending the chimera approach to other conformations and antigenic sites, the chimeric proteins F‐410, F‐411, and F‐412 of Fig EV1 were produced.…”
Section: Resultsmentioning
confidence: 99%
“…Both F‐410 and F‐411 retained reactivity with three mAbs (D25, AM22, and 5C4) that recognize epitopes in the prefusion‐specific site Ø of hRSV F (McLellan et al , 2013b). The two chimeric proteins also reacted with two mAbs (14402 and 11569) specific for the recently identified prefusion hRSV F antigenic site V (Gilman et al , 2016).…”
Section: Resultsmentioning
confidence: 99%
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“…While pre-and postfusion forms of F have been crystallized, many of the specific events that underlie the process are still unknown (14,15). Since HRA and HRB have been extensively studied due to their role in the formation of the critical 6HB, we shifted our focus to a heptad repeat in the F 2 subunit (aa 75 to 97), referred to herein as HRC, which has remained largely uncharacterized in RSV.…”
mentioning
confidence: 99%