Lipid composition modulates the interaction of peptides deriving from herpes simplex virus type I glycoproteins B and H with biomembranes.
نویسندگان
چکیده
Lipid membranes play a key role in the viral life cycle. Enveloped viruses particularly require a sequence of fusion and fission events between the viral envelope and the target membranes for entry into the cell and egress from it. These processes are controlled by one or more viral glycoproteins that undergo conformational changes favoring the necessary micro- and mesoscopic lipid re-arrangements. Multiple regions from these glycoproteins are thought to interact with the membranes, according to a concerted mechanism, in order to generate the distortion necessary for fusion. In this work, we perform an EPR study on the role played by the membrane composition in tuning the interaction between lipid bilayers and two peptides, gH626-644 and gB632-650, that are highly fusogenic fragments of the gH and gB glycoproteins of herpes simplex virus. Our results show that both peptides interact with lipid bilayers, perturbing the local lipid packing. gH626-644 localizes close to the hydrophilic bilayer surface, while gB632-650 penetrates deeply into the membrane. Chain perturbation by the peptides increases in the presence of charged phospholipids. Finally, cholesterol does not alter the ability of gB632-650 to penetrate deeply in the membrane, whereas it limits penetration of the gH626-644 peptide to the more external layer. The different modes of interaction result in a higher fusogenic ability of gB632-650 towards cholesterol-enriched membranes, as demonstrated by lipid mixing assays. These results suggest that the mechanism of action of the gH and gB glycoproteins is modulated by the properties and composition of the phospholipid bilayer.
منابع مشابه
Immunogenicity and Efficacy of Baculovirus Derived Glycoprotein D of Herpes Simplex Virus Type-I in Mice
متن کامل
Up-Regulation of Integrinsn α2β1 and α3β1 Expression in Human Foreskin Fibroblast Cells after In-Vitro Infection with Herpes Simplex Virus Type 1
The interaction of Herpes Simplex Virus type 1 (HSV-1) with human fetal foreskin fibroblast (HFFF) cell was studied using a recent isolate of HSV-1 which was propagated in Hep-2 cells. HFFF cells were challenged with HSV-1 with a multiplicity of infection (MOI) of 1 virus/cell for 24 hours. Flow cytometric analysis demonstrated that HSV-1 challenged HFFF cells expressed increased levels of α2β1...
متن کاملDetection of Herpes Simplex Virus Antibodies Using the Whole Virus and Recombinant gD
Background and Aims: Herpes simplex virus type 1 (HSV1) remains a potentially serious health problem world wide. All infected people, including asymptomatic ones, are potential sources for virus transmission. Virus envelope contains at least 13 glycoproteins, which glycoprotein D is the major target of immune responses. The aim of this study was development of a specific method that is a more...
متن کاملThe Changing Epidemiology of Herpes Simplex Virus Type 1 Infection: The Associated Effects on the Incidence of Ocular Herpes
Herpes simplex virus type 1 (HSV-1) with a worldwide distribution has been reported in all human populations, resulting in a clinical spectrum of infections. Although HSV type 2 (HSV-2) is known as the most common cause of genital herpes, an increasing number of cases with genital herpes are caused by HSV-1. The present study aimed to discuss the changes in the epidemiology of HSV-1 infection i...
متن کاملLoop-Mediated Isothermal Amplification (LAMP) for the Rapid Diagnosis of Herpes Simplex Virus Type 1 (HSV-1)
Background and Aims: considering difficulties in usual laboratory methods in detection of viral infections, improved DNA-based diagnostic techniques are more reliable. Loop mediated isothermal amplification method (LAMP) is a nucleic acid amplification method that amplifies DNA using six primers which has been developed to diagnose viruses as a rapid and high efficiency test. In this study, the...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- Biochimica et biophysica acta
دوره 1808 10 شماره
صفحات -
تاریخ انتشار 2011