Modeling of 3D Structure of Chimeric Constructs Based on Hemagglutinin of Influenza Virus and Immunogenic Epitopes of Streptococcus Agalactiae

Autor: Irina Isakova-Sivak, Larisa Rudenko, G. F. Leont’eva, E. A. Fedorova, Daniil Korenkov, Tatiana Kotomina, Tatiana Smolonogina, Alexander Suvorov
Rok vydání: 2018
Předmět:
Models
Molecular
Protein Conformation
alpha-Helical
0301 basic medicine
Influenza vaccine
Recombinant Fusion Proteins
Gene Expression
Hemagglutinin (influenza)
Hemagglutinin Glycoproteins
Influenza Virus
Biology
medicine.disease_cause
General Biochemistry
Genetics and Molecular Biology
Epitope
Virus
Streptococcus agalactiae
law.invention
03 medical and health sciences
law
Streptococcal Infections
medicine
Animals
Humans
Protein Interaction Domains and Motifs
Amino Acid Sequence
Antigens
Bacterial
Vaccines
Synthetic
Binding Sites
030102 biochemistry & molecular biology
Immunogenicity
Streptococcal Vaccines
Membrane Proteins
General Medicine
Vector vaccine
Virology
030104 developmental biology
biology.protein
Recombinant DNA
Epitopes
B-Lymphocyte
Protein Conformation
beta-Strand
Protein Binding
Zdroj: Bulletin of Experimental Biology and Medicine. 164:743-748
ISSN: 1573-8221
0007-4888
Popis: A project of an experimental recombinant vector vaccine for prevention of diseases caused by pathogenic streptococci based on ScaAB lipoprotein of Streptococcus agalactiae and a coldadapted strain of live influenza vaccine as a vector was developed. The sequence of ScaAB lipoprotein was analyzed and fragments forming immunodominant epitopes were determined. Chimeric molecules of influenza virus hemagglutinin H7 carrying insertions of bacterial origin were constructed. Based on the results of simulation, the most promising variants were selected; they represented fragments of lipoprotein ScaAB lacking N-terminal domain bound to hemagglutinin via a flexible linker. These insertions should minimally modulate the properties of the influenza strain, while retaining potential immunogenicity to a wide group of pathogenic streptococci.
Databáze: OpenAIRE
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