6GOL

Three dimensional structure of a novel influenza hemagglutinin tri-stalk protein

Summary for 6GOL

• Entry DOI: 10.2210/pdb6gol/pdb
• Descriptor: Hemagglutinin tri-stalk (2 entities in total)
• Functional Keywords: hemagglutinin stem, long alpha helix, influenza, post-fusion conformation, tri-stalk protein, viral protein
• Biological source: Influenza A virus (A/California/VRDL69/2009(H1N1))
• Total number of polymer chains: 1
• Total formula weight: 8554.57

Authors

Kirsteina, A.,Kazaks, A.,Tars, K. (deposition date: 2018-06-01, release date: 2018-10-10, Last modification date: 2024-01-17)

Primary citation

Lu, I.N.,Kirsteina, A.,Farinelle, S.,Willieme, S.,Tars, K.,Muller, C.P.,Kazaks, A.
Structure and applications of novel influenza HA tri-stalk protein for evaluation of HA stem-specific immunity.
PLoS ONE, 13:e0204776-e0204776, 2018

PubMed 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.

PubMed: 30261065
DOI: 10.1371/journal.pone.0204776

Experimental method

X-RAY DIFFRACTION (1.7 Å)