tetano
Editor, Senior Moderator
Vaccine
Volume 30, Issue 51, 7 December 2012, Pages 7368?7373
Fourth ESWI Influenza Conference
Cover image
Distribution of surface glycoproteins on influenza A virus determined by electron cryotomography
Sebastian Wasilewski,
Lesley J. Calder,
Tim Grant,
Peter B. RosenthalCorresponding author contact information, E-mail the corresponding author
Division of Physical Biochemistry, MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London, NW7 1AA, United Kingdom
http://dx.doi.org/10.1016/j.vaccine.2012.09.082
Abstract
We use electron cryotomography to reconstruct virions of two influenza A H3N2 virus strains. The maps reveal the structure of the viral envelope containing hemagglutinin (HA) and neuraminidase (NA) glycoproteins and the virus interior containing a matrix layer and an assembly of ribonucleoprotein particles (RNPs) that package the genome. We build a structural model for the viral surface by locating copies of the X-ray structure of the HA ectodomain into density peaks on the virus surface. We calculate inter-glycoprotein distances and the fractional volume occupied by glycoproteins. The models suggest that for typical HA densities on virus, Fabs can bind to epitopes on the HA stem domain. The models also show how membrane curvature may influence the number of glycoproteins that can simultaneously interact with a target surface of receptors.
Highlights
► Cryotomography of influenza A virus reveals a polarized structure. ► 3D models for the virus envelope are built using glycoprotein X-ray structures. ► Inter-glycoprotein distances and fractional surface volumes are calculated. ► Accessibility of the HA stem domain to neutralizing antibodies is assessed. ► Viral membrane curvature may constrain interaction with a surface of receptors.
http://www.sciencedirect.com/science/article/pii/S0264410X12014260
Volume 30, Issue 51, 7 December 2012, Pages 7368?7373
Fourth ESWI Influenza Conference
Cover image
Distribution of surface glycoproteins on influenza A virus determined by electron cryotomography
Sebastian Wasilewski,
Lesley J. Calder,
Tim Grant,
Peter B. RosenthalCorresponding author contact information, E-mail the corresponding author
Division of Physical Biochemistry, MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London, NW7 1AA, United Kingdom
http://dx.doi.org/10.1016/j.vaccine.2012.09.082
Abstract
We use electron cryotomography to reconstruct virions of two influenza A H3N2 virus strains. The maps reveal the structure of the viral envelope containing hemagglutinin (HA) and neuraminidase (NA) glycoproteins and the virus interior containing a matrix layer and an assembly of ribonucleoprotein particles (RNPs) that package the genome. We build a structural model for the viral surface by locating copies of the X-ray structure of the HA ectodomain into density peaks on the virus surface. We calculate inter-glycoprotein distances and the fractional volume occupied by glycoproteins. The models suggest that for typical HA densities on virus, Fabs can bind to epitopes on the HA stem domain. The models also show how membrane curvature may influence the number of glycoproteins that can simultaneously interact with a target surface of receptors.
Highlights
► Cryotomography of influenza A virus reveals a polarized structure. ► 3D models for the virus envelope are built using glycoprotein X-ray structures. ► Inter-glycoprotein distances and fractional surface volumes are calculated. ► Accessibility of the HA stem domain to neutralizing antibodies is assessed. ► Viral membrane curvature may constrain interaction with a surface of receptors.
http://www.sciencedirect.com/science/article/pii/S0264410X12014260