Structure and applications of novel influenza HA tri-stalk protein for evaluation of HA stemspecific immunity

I. Na Lu, Anna Kirsteina, Sophie Farinelle, Stephanie Willieme, Kaspars Tars, Claude P. Muller, Andris Kazaks

Research output: Contribution to journalArticleResearchpeer-review

8 Citations (Scopus)

Abstract

Long alpha helix (LAH) from influenza virus hemagglutinin (HA) stem or stalk domain is one of the most conserved influenza virus antigens. Expression of N-terminally extended LAH in E. coli leads to assembly of α-h elical homotrimer which is structurally nearly identical to the corresponding region of post-fusion form of native HA. This novel tri-stalk protein was able to differentiate between group 1 and 2 influenza in ELISA with virus-infected mice sera. It was also successfully applied for enzyme-linked immunospot assay to estimate the number of HA stem-reactive antibody (Ab)-secreting cells in mice. An in-house indirect ELISA was developed using a HA tri-stalk protein as a coating antigen for evaluation of HA stem-specific Ab levels in human sera collected in Luxembourg from 211 persons with occupational exposure to swine before the pandemic H1N1/09 virus had spread to Western Europe. Our results show that 70% of these pre-pandemic sera are positive for HA stem-specific Abs. In addition, levels of HA stem-specific Abs have positive correlation with the corresponding IgG titers and neutralizing activities against pandemic H1N1/09 virus.

Original languageEnglish
Article numbere0204776
JournalPLoS ONE
Volume13
Issue number9
DOIs
Publication statusPublished - Sep 2018

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