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J Virol Methods. 2015 Nov;224:1-8. doi: 10.1016/j.jviromet.2015.08.002. Epub 2015 Aug 12.

Generation of monoclonal antibodies specific of the postfusion conformation of the Pneumovirinae fusion (F) protein.

Author information

1
Unidad de Biología Viral, Centro Nacional de Microbiología and CIBER de Enfermedades Respiratorias, 28220 Madrid, Spain.
2
Unidad de Microscopía Electrónica y Confocal, Instituto de Salud Carlos III, Majadahonda, 28220 Madrid, Spain.
3
Unidad de Biología Viral, Centro Nacional de Microbiología and CIBER de Enfermedades Respiratorias, 28220 Madrid, Spain. Electronic address: cpalomo@isciii.es.
4
Unidad de Biología Viral, Centro Nacional de Microbiología and CIBER de Enfermedades Respiratorias, 28220 Madrid, Spain. Electronic address: jmelero@isciii.es.

Abstract

Paramyxovirus entry into cells requires fusion of the viral and cell membranes mediated by one of the major virus glycoproteins, the fusion (F) glycoprotein which transits from a metastable pre-fusion conformation to a highly stable post-fusion structure during the membrane fusion process. F protein refolding involves large conformational changes of the protein trimer. One of these changes results in assembly of two heptad repeat sequences (HRA and HRB) from each protomer into a six-helix bundle (6HB) motif. To assist in distinguishing pre- and post-fusion conformations of the Pneumovirinae F proteins, and as extension of previous work (Palomo et al., 2014), a general strategy was designed to obtain polyclonal and particularly monoclonal antibodies specific of the 6HB motif of the Pneumovirinae fusion protein. The antibodies reported here should assist in the characterization of the structural changes that the F protein of human metapneumovirus or respiratory syncytial virus experiences during the process of membrane fusion.

KEYWORDS:

Conformation specific antibodies; Fusion proteins; Pneumovirinae

PMID:
26275682
DOI:
10.1016/j.jviromet.2015.08.002
[Indexed for MEDLINE]

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