Characterization of the role of N-glycosylation sites in the respiratory syncytial virus fusion protein in virus replication, syncytium formation and antigenicity

Leemans, Annelies; Boeren, Marlies; Gucht, Winke Van der; Martinet, Wim; Caljon, Guy; Maes, Louis; Cos, Paul; Delputte, Peter

doi:10.1016/j.virusres.2019.04.006

Cited by 22 publications

(17 citation statements)

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“…Previous studies showed that a large part of the genetic variability between RSV strains comes from changes in the O-glycosylation profile and that this may be associated with an evolutionary mechanism of immune response evasion [ 58 ]. Here, we investigated and listed strain amino acid substitutions and also those shared within and between clusters.…”

Section: Discussionmentioning

confidence: 99%

Seasonality, molecular epidemiology, and virulence of Respiratory Syncytial Virus (RSV): A perspective into the Brazilian Influenza Surveillance Program

et al. 2021

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Background Respiratory Syncytial Virus (RSV) is the main cause of pediatric morbidity and mortality. The complex evolution of RSV creates a need for worldwide surveillance, which may assist in the understanding of multiple viral aspects. Objectives This study aimed to investigate RSV features under the Brazilian Influenza Surveillance Program, evaluating the role of viral load and genetic diversity in disease severity and the influence of climatic factors in viral seasonality. Methodology We have investigated the prevalence of RSV in children up to 3 years of age with severe acute respiratory infection (SARI) in the state of Espirito Santo (ES), Brazil, from 2016 to 2018. RT-qPCR allowed for viral detection and viral load quantification, to evaluate association with clinical features and mapping of local viral seasonality. Gene G sequencing and phylogenetic reconstruction demonstrated local genetic diversity. Results Of 632 evaluated cases, 56% were caused by RSV, with both subtypes A and B co-circulating throughout the years. A discrete inverse association between average temperature and viral circulation was observed. No correlation between viral load and disease severity was observed, but children infected with RSV-A presented a higher clinical severity score (CSS), stayed longer in the hospital, and required intensive care, and ventilatory support more frequently than those infected by RSV-B. Regarding RSV diversity, some local genetic groups were observed within the main genotypes circulation RSV-A ON1 and RSV-B BA, with strains showing modifications in the G gene amino acid chain. Conclusion Local RSV studies using the Brazilian Influenza Surveillance Program are relevant as they can bring useful information to the global RSV surveillance. Understanding seasonality, virulence, and genetic diversity can aid in the development and suitability of antiviral drugs, vaccines, and assist in the administration of prophylactic strategies.

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Section: Discussionmentioning

confidence: 99%

Seasonality, molecular epidemiology, and virulence of Respiratory Syncytial Virus (RSV): A perspective into the Brazilian Influenza Surveillance Program

et al. 2021

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“…The RSV F has five N -glycosylation sites, which are N27 and N70 located in the F2 subunit, N116 and N126 in the p27 peptide, as well as N500 in the F1 subunit. Every single N -glycosylation site in the RSV F protein is not dispensible for virus replication, but they have synergistic contribution to the efficiency of viral infection [ 96 ]. The virus can not replicate if all the N -glycans in the RSV F protein are removed.…”

Section: The Roles Of Glycosylation On Viral Structural Proteinsmentioning

confidence: 99%

“…The virus can not replicate if all the N -glycans in the RSV F protein are removed. Data have demonstrated that the N-glycan at the N500 position is essential for syncytium formation in RSV-infected Hep-2 cells [ 96 ]. In addition, the frequency of syncytia formation in RSV F N116Q-infected cells was also significantly reduced, indicating that N-glycosylation at N116 affects syncytia formation.…”

Section: The Roles Of Glycosylation On Viral Structural Proteinsmentioning

confidence: 99%

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Glycosylation of viral proteins: Implication in virus–host interaction and virulence

et al. 2022

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Glycans are among the most important cell molecular components. However, given their structural diversity, their functions have not been fully explored. Glycosylation is a vital post-translational modification for various proteins. Many bacteria and viruses rely on N -linked and O-linked glycosylation to perform critical biological functions. The diverse functions of glycosylation on viral proteins during viral infections, including Dengue, Zika, influenza, and human immunodeficiency viruses as well as coronaviruses have been reported. N -linked glycosylation is the most common form of protein modification, and it modulates folding, transportation and receptor binding. Compared to N -linked glycosylation, the functions of O-linked viral protein glycosylation have not been comprehensively evaluated. In this review, we summarize findings on viral protein glycosylation, with particular attention to studies on N-linked glycosylation in viral life cycles. This review informs the development of virus-specific vaccines or inhibitors.

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“…A commonly used method to restrict off-target responses is to introduce novel predicted N-linked glycosylation (PNG) sites on viral surface proteins to "shield" or occlude undesired epitopes. Glycans are naturally present on viral envelope proteins and play key roles in stability, pathogenicity, and immunogenicity, as well as escape from immune surveillance [82][83][84][85][86][87][88][89][90] . Overall glycosylation patterns can affect antigen processing, delivery into GCs, and breadth of elicited responses [91][92][93][94][95][96][97][98][99][100][101] .…”

Section: Occlusion Of Off-target Epitopesmentioning

confidence: 99%

Protein engineering strategies for rational immunogen design

Caradonna

Schmidt

2021

npj Vaccines

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Antibody immunodominance refers to the preferential and asymmetric elicitation of antibodies against specific epitopes on a complex protein antigen. Traditional vaccination approaches for rapidly evolving pathogens have had limited success in part because of this phenomenon, as elicited antibodies preferentially target highly variable regions of antigens, and thus do not confer long lasting protection. While antibodies targeting functionally conserved epitopes have the potential to be broadly protective, they often make up a minority of the overall repertoire. Here, we discuss recent protein engineering strategies used to favorably alter patterns of immunodominance, and selectively focus antibody responses toward broadly protective epitopes in the pursuit of next-generation vaccines for rapidly evolving pathogens.

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Characterization of the role of N-glycosylation sites in the respiratory syncytial virus fusion protein in virus replication, syncytium formation and antigenicity

Cited by 22 publications

References 53 publications

Seasonality, molecular epidemiology, and virulence of Respiratory Syncytial Virus (RSV): A perspective into the Brazilian Influenza Surveillance Program

Seasonality, molecular epidemiology, and virulence of Respiratory Syncytial Virus (RSV): A perspective into the Brazilian Influenza Surveillance Program

Glycosylation of viral proteins: Implication in virus–host interaction and virulence

Protein engineering strategies for rational immunogen design

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