Advanced search
Start date
(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

SARS-CoV fusion peptides induce membrane surface ordering and curvature

Full text
Basso, Luis G. M. ; Vicente, Eduardo F. ; Crusca, Jr., Edson ; Cilli, Eduardo M. ; Costa-Filho, Antonio J.
Total Authors: 5
Document type: Journal article
Source: SCIENTIFIC REPORTS; v. 6, NOV 28 2016.
Web of Science Citations: 9

Viral membrane fusion is an orchestrated process triggered by membrane-anchored viral fusion glycoproteins. The S2 subunit of the spike glycoprotein from severe acute respiratory syndrome (SARS) coronavirus (CoV) contains internal domains called fusion peptides (FP) that play essential roles in virus entry. Although membrane fusion has been broadly studied, there are still major gaps in the molecular details of lipid rearrangements in the bilayer during fusion peptide-membrane interactions. Here we employed differential scanning calorimetry (DSC) and electron spin resonance (ESR) to gather information on the membrane fusion mechanism promoted by two putative SARS FPs. DSC data showed the peptides strongly perturb the structural integrity of anionic vesicles and support the hypothesis that the peptides generate opposing curvature stresses on phosphatidylethanolamine membranes. ESR showed that both FPs increase lipid packing and head group ordering as well as reduce the intramembrane water content for anionic membranes. Therefore, bending moment in the bilayer could be generated, promoting negative curvature. The significance of the ordering effect, membrane dehydration, changes in the curvature properties and the possible role of negatively charged phospholipids in helping to overcome the high kinetic barrier involved in the different stages of the SARS-CoV-mediated membrane fusion are discussed. (AU)

FAPESP's process: 14/00206-0 - Structure and function of SARS-CoV spike glycoprotein fusion peptides
Grantee:Luís Guilherme Mansor Basso
Support type: Scholarships in Brazil - Post-Doctorate
FAPESP's process: 15/18390-5 - Electron magnetic resonance in molecular biophysics: new and old looks to new and old problems
Grantee:Antonio José da Costa Filho
Support type: Regular Research Grants
FAPESP's process: 09/10997-7 - Interactions between model membranes and fusion peptides derived from SARS CoV glycoprotein s
Grantee:Luís Guilherme Mansor Basso
Support type: Scholarships in Brazil - Doctorate
FAPESP's process: 10/12953-4 - Structural determination of the C-terminal domains of septins SEPT2 and SEPT4 and protein interaction with alpha-synuclein by NMR
Grantee:Edson Crusca Junior
Support type: Scholarships in Brazil - Post-Doctorate
FAPESP's process: 08/57910-0 - National Institute of Structural Biotechnology and Medicinal Chemistry in Infectious Diseases
Grantee:Richard Charles Garratt
Support type: Research Projects - Thematic Grants