Abstract

A significant increase in the number of viruses causing unexpected illnesses and epidemics among humans, wildlife and livestock has been observed in recent years. These new or re-emerging viruses have often caught the scientific community off-guard, without sufficient knowledge to combat them, as shown by the current coronavirus pandemic. The bunyaviruses, together with the flaviviruses and filoviruses, are the major etiological agents of viral hemorrhagic fever, and several of them have been listed as priority pathogens by the World Health Organization for which insufficient countermeasures exist. Based on new techniques allowing rapid analysis of the repertoire of protective antibodies induced during infection, combined with atomic-level structural information on viral surface proteins, structural vaccinology is now instrumental in the combat against newly emerging threats, as it allows rapid rational design of novel vaccine antigens. Here, we discuss the contribution of structural vaccinology and the current challenges that remain in the search for an efficient vaccine against some of the deadliest bunyaviruses.

Highlights

  • A significant increase in the number of viruses causing unexpected illnesses and epidemics among humans, wildlife and livestock has been observed in recent years

  • Progress in the fields of human immunology and structural biology facilitated the generation of structural data on protein complexes and led to the development of a new approach to design better immunogens, commonly referred to as structural vaccinology

  • In 1995, a DNA-based vaccine against La Crosse virus coding for Gn/Gc glycoproteins was shown to elicit a protective immune response mediated by neutralizing antibodies and CD4+ T cells in a mouse model [61]

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Summary

Introduction

A significant increase in the number of viruses causing unexpected illnesses and epidemics among humans, wildlife and livestock has been observed in recent years. Both glycoproteins interact to outer lattice covering the virus, which plays a major role in particle assembly, mediates all of the entry form a metastable spike comprising three or four Gn/Gc heterodimers, depending on the steps into permissive cells, and is the sole target of neutralizing antibodies family.

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