Overexpression of Ebola virus envelope GP1 protein
نویسندگان
چکیده
منابع مشابه
Comprehensive Functional Analysis of N-Linked Glycans on Ebola Virus GP1
UNLABELLED Ebola virus (EBOV) entry requires the virion surface-associated glycoprotein (GP) that is composed of a trimer of heterodimers (GP1/GP2). The GP1 subunit contains two heavily glycosylated domains, the glycan cap and the mucin-like domain (MLD). The glycan cap contains only N-linked glycans, whereas the MLD contains both N- and O-linked glycans. Site-directed mutagenesis was performed...
متن کاملPurification of monoclonal antibody against Ebola GP1 protein expressed in Nicotiana benthamiana.
Monoclonal antibodies (mAbs) are one of the fastest growing drug molecules targeting the treatment of diseases ranging from arthritis, immune disorders, and infectious diseases to cancer. Due to its unique application principle, antibodies are commonly produced in large quantities. Plants, such as Nicotiana benthamiana, offer a unique production platform for bio-therapeutics due to their abilit...
متن کاملligand screening approach to find potential inhibitors of gp1 from ebola virus
ebola is one of the members of filoviruses family. it causes severe hemorrhagic with the human mortality rate of 50-90%. in the initial steps of infection, it enters the host cell by glyco protein1 (gp1). gp1 is a big subunit with the molecular weight of 130 kda. its n-terminal domain is responsible for attaching the host cell. in the present study, a database containing 100.000 drug like chemi...
متن کاملDengue virus type-3 envelope protein domain III; expression and immunogenicity
Objective(s): Production of a recombinant and immunogenic antigen using dengue virus type-3 envelope protein is a key point in dengue vaccine development and diagnostic researches. The goals of this study were providing a recombinant protein from dengue virus type-3 envelope protein and evaluation of its immunogenicity in mice. Materials and Methods: Multiple amino acid sequences of different i...
متن کاملOverexpression of Full-Length Core Protein of Hepatitis C Virus by Escherichia coli Cultivated in Stirred Tank Fermentor
The mature core protein of the Hepatitis C virus (HCVC173) carrying pelB as a signal peptide (PelB::core) was overexpressed in Escherichia coli as 18% and 23.3% of the host’s total protein, in flask and fermentor cultivation, respectively. A final specific yield of 25 ± 1 mg HCVC173/g dry cell weight and an overallproductivity of 51±1 mg HCVC173/l/h were obtained in the stirred-tank ferme...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Protein Expression and Purification
سال: 2017
ISSN: 1046-5928
DOI: 10.1016/j.pep.2017.04.010