Palivizumab‐Resistant Human Respiratory Syncytial Virus Infection in Infancy

Adams, Ortwin; Bonzel, Linda; Kovacevic, Alexander; Mayatepek, Ertan; Hoehn, Thomas; Vogel, Markus

doi:10.1086/653534

Cited by 63 publications

(47 citation statements)

References 15 publications

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“…The determination of epitopes targeted by antibodies is useful for understanding virus escape (1), antibody optimization (2,3) and epitope-based design of vaccines (4). Structure determination (by, e.g.…”

Section: Introductionmentioning

confidence: 99%

NEP: web server for epitope prediction based on antibody neutralization of viral strains with diverse sequences

Chuang¹,

Liou²,

Kwong³

et al. 2014

Nucleic Acids Research

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Delineation of the antigenic site, or epitope, recognized by an antibody can provide clues about functional vulnerabilities and resistance mechanisms, and can therefore guide antibody optimization and epitope-based vaccine design. Previously, we developed an algorithm for antibody-epitope prediction based on antibody neutralization of viral strains with diverse sequences and validated the algorithm on a set of broadly neutralizing HIV-1 antibodies. Here we describe the implementation of this algorithm, NEP (Neutralization-based Epitope Prediction), as a web-based server. The users must supply as input: (i) an alignment of antigen sequences of diverse viral strains; (ii) neutralization data for the antibody of interest against the same set of antigen sequences; and (iii) (optional) a structure of the unbound antigen, for enhanced prediction accuracy. The prediction results can be downloaded or viewed interactively on the antigen structure (if supplied) from the web browser using a JSmol applet. Since neutralization experiments are typically performed as one of the first steps in the characterization of an antibody to determine its breadth and potency, the NEP server can be used to predict antibody-epitope information at no additional experimental costs. NEP can be accessed on the internet at http://exon.niaid.nih.gov/nep.

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Section: Introductionmentioning

confidence: 99%

NEP: web server for epitope prediction based on antibody neutralization of viral strains with diverse sequences

Chuang¹,

Liou²,

Kwong³

et al. 2014

Nucleic Acids Research

View full text Add to dashboard Cite

show abstract

“…The scarce information on patients that is available comes from studies on individuals who received PZ, and it has been reported recently that a PZ-resistant HRSV isolated from patients who had received PZ had amino acid substitutions at positions 272, 275 and 276 [47][48][49]. Also, a study of natural polymorphisms in the F protein of HRSV showed that mutations Asn262Asp and Ser275Phe isolated from immunoprophylaxis-naïve subjects are associated with resistance to palivizumab [48].…”

Section: Discussionmentioning

confidence: 99%

Selection and characterization of human respiratory syncytial virus escape mutants resistant to a polyclonal antiserum raised against the F protein

et al. 2012

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“…1 40) and was dominant in Canada between 2008 and 2010 41) . Adams et al showed that the N276S mutation in RSV -A leads to a decrease in NT activity against palivizumab 47) . This mutant virus was isolated from preterm infants 4 months old who were administered palivizumab but were treated in an intensive care unit for RSV infection.…”

Section: Palivizumab Resistancementioning

confidence: 99%

“…On the other hand, they also reported that the detection frequency of palivizumab -resistant mutations in RSV isolated from patients receiving palivizumab treatment was 5.4% 43) . The amino acid at position 276 of the F protein is generally asparagine (N) for RSV -A and serine (S) for RSV -B 40,47) . It is possible that the N276S mutation in RSV -A and S276N mutation in RSV -B appeared due to hybridization between the subgroups, natural mutation and so on.…”

Section: Palivizumab Resistancementioning

confidence: 99%

Neutralizing epitopes of RSV and palivizumab resistance in Japan

Hashimoto¹,

Hosoya²

2017

FJMS

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Respiratory Syncytial Virus (RSV) is one of the most important viral pathogen related to acute lower respiratory infection in young children. The virus surface envelope contains the G, F, and SH proteins as spike proteins. The F protein is considered to be a major antigenic target for the neutralizing (NT) epitope as only the F protein is essential for cell infection among the three viral envelope proteins, and it is more highly conserved than the G protein. Recently, four antigenic targets related to NT activity have been reported ; site I, site II, site IV, and site zero (0). Site II is the target for palivizumab used throughout the world to suppress severe RSV infection as passive immunity in high -risk children since 1998. Under the recent conditions in which indications for palivizumab administered subjects are being expanded, palivizumab -resistant mutations have been confirmed overseas in children with RSV infection, although they remain infrequent. Therefore, continuous genetic analysis of the palivizumab -binding region of the F protein is necessary. In addition, as vaccine development progresses, RSV infection control is expected to improve greatly over the next decade.

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Palivizumab‐Resistant Human Respiratory Syncytial Virus Infection in Infancy

Cited by 63 publications

References 15 publications

NEP: web server for epitope prediction based on antibody neutralization of viral strains with diverse sequences

NEP: web server for epitope prediction based on antibody neutralization of viral strains with diverse sequences

Selection and characterization of human respiratory syncytial virus escape mutants resistant to a polyclonal antiserum raised against the F protein

Neutralizing epitopes of RSV and palivizumab resistance in Japan

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