Comparison of the nucleotide and deduced amino acid sequences of the structural protein genes of the yellow fever 17DD vaccine strain from Senegal with those of other yellow fever vaccine viruses

Vaccine ◽  
1993 ◽  
Vol 11 (6) ◽  
pp. 679-681 ◽  
Author(s):  
A.D. Jennings ◽  
J.E. Whitby ◽  
P.D. Minor ◽  
A.D.T. Barrett
Keyword(s):  
Amino Acid ◽  
Yellow Fever ◽  
Vaccine Strain ◽  
Amino Acid Sequences ◽  
Yellow Fever Vaccine ◽  
Structural Protein

scholarly journals Expression and characterisation of the ryegrass mottle virus non-structural proteins

2010 ◽  
Vol 64 (5-6) ◽  
pp. 215-222
Author(s):  
Ina Baļķe ◽  
Gunta Resēviča ◽  
Dace Skrastiņa ◽  
Andris Zeltiņš
Keyword(s):  
Amino Acid ◽  
Expression System ◽  
Protein Structures ◽  
Amino Acid Sequences ◽  
Host Cells ◽  
Structural Proteins ◽  
Mottle Virus ◽  
Expression Vectors ◽  
Structural Protein ◽  
E Coli

Expression and characterisation of the ryegrass mottle virus non-structural proteins The Ryegrass mottle virus (RGMoV) single-stranded RNA genome is organised into four open reading frames (ORF) which encode several proteins: ORF1 encodes protein P1, ORF2a contains the membrane-associated 3C-like serine protease, genome-linked protein VPg and a P16 protein gene. ORF2b encodes replicase RdRP and the only structural protein, coat protein, is synthesised from ORF3. To obtain the non-structural proteins in preparative quantities and to characterise them, the corresponding RGMoV gene cDNAs were cloned in pET- and pColdI-derived expression vectors and overexpressed in several E. coli host cells. For protease and RdRP, the best expression system containing pColdI vector and E. coli WK6 strain was determined. VPg and P16 proteins were obtained from the pET- or pACYC- vectors and E. coli BL21 (DE3) host cells and purified using Ni-Sepharose affinity chromatography. Attempts to crystallize VPg and P16 were unsuccessful, possibly due to non-structured amino acid sequences in both protein structures. Methods based on bioinformatic analysis indicated that the entire VPg domain and the C-terminal part of the P16 contain unstructured amino acid stretches, which possibly prevented the formation of crystals.

scholarly journals Using the vaccinia virus MVA strain for developing recombinant vector vaccines against current arboviral infections

2021 ◽  
Vol 98 (5) ◽  
pp. 579-587
Author(s):  
L. F. Stovba ◽  
V. T. Krotkov ◽  
S. A. Melnikov ◽  
D. I. Paveliev ◽  
N. K. Chernikova ◽  
...  
Keyword(s):  
Yellow Fever ◽  
Viral Infections ◽  
Protective Efficacy ◽  
Preventive Treatment ◽  
Hemorrhagic Fever ◽  
Yellow Fever Vaccine ◽  
Structural Protein ◽  
Valley Fever ◽  
Viral Glycoproteins ◽  
Vector Borne

Epidemic vector-borne viral infections pose a serious threat to public health worldwide. There is currently no specific preventive treatment for most of them. One of the promising solutions for combating viral fevers is development of vector vaccines, including MVA-based vaccines, which have virtually no adverse side effects. The safety of the MVA strain and absent reactogenicity of recombinant MVA vaccines have been supported by many clinical trials.The article focuses on test results for similar preventive products against viral fevers: Crimean-Congo hemorrhagic fever, Rift Valley fever, yellow fever, Chikungunya and Zika fevers.Their immunogenicity was evaluated on immunocompetent and immunocompromised white mice; their protective efficacy was assessed on immunocompromised white mice deficient in IFN-α/β receptors, that are used for experimental modeling of the infection. Nearly all the new recombinant vaccines expressing immunodominant antigens demonstrated 100% protective efficacy. It has been found that although the vaccine expressing Zika virus structural proteins induced antibodies against specific viral glycoproteins, it can be associated with high risks when used for prevention of Zika fever in individuals who had dengue fever in the past, due to the phenomenon known as antibody-dependent enhancement of infection, which can occur in diseases caused by antigenically related flaviruses. For this reason, the vaccine expressing non-structural protein 1 (NS1) was developed for vaccination against Zika fever.The yellow fever vaccine developed on the MVA platform had immunogenicity similar to that of the commercial 17D vaccine, outperforming the latter in safety.

scholarly journals Sequence of the non-structural protein gene encoded by RNA1 of striped jack nervous necrosis virus

1999 ◽  
Vol 80 (11) ◽  
pp. 3019-3022 ◽  
Author(s):  
Takahiro Nagai ◽  
Toyohiko Nishizawa
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequences ◽  
Nervous Necrosis Virus ◽  
Structural Protein ◽  
Necrosis Virus ◽  
Rna Molecules ◽  
Viral Nervous Necrosis ◽  
The Family ◽  
Amino Acid Levels ◽  
Structural Protein Gene

Striped jack nervous necrosis virus (SJNNV), the causative agent of viral nervous necrosis in marine fish, is a member of the family Nodaviridae whose genome consists of two positive-sense RNA molecules encapsidated in a single virion. In this study, the nucleotide sequence of SJNNV RNA1 was determined. The SJNNV RNA1 was 3081 bases long and contained a single ORF encoding 983 aa of approximately 110 kDa. The sequence identities between RNA1 of SJNNV and RNA1 of insect nodaviruses were 28% at the nucleotide and amino acid levels, although the conserved motifs for the RNA-dependent RNA polymerase were located at almost the same positions in the amino acid sequences. The present study, together with our previous work on SJNNV RNA2, suggests that a new genus, Piscinodavirus, should be created in the family Nodaviridae.

scholarly journals Biochemical features of parvovirus B19 genovariant 1a2 dominating during the incidence rise in Belarus

2020 ◽  
Vol 17 (2) ◽  
pp. 211-220
Author(s):  
M. A. Yermalovich ◽  
V. V. Khrustalev ◽  
T. A. Khrustaleva ◽  
V. V. Poboinev ◽  
E. O. Samoilovich
Keyword(s):  
Amino Acid ◽  
Parvovirus B19 ◽  
Three Dimensional ◽  
Amino Acid Sequences ◽  
Dimensional Structure ◽  
Amino Acid Substitutions ◽  
Structural Protein ◽  
Mutational Pressure ◽  
Amino Acid Variability ◽  
Unique Amino Acid

Two genovariants (1a1 and 1a2) are distinguished among Human parvovirus B19 (B19P) of subgenotype 1a, of which 1a2 was predominantly distributed during the incidence rise in Belarus. The aim of this study was a comparative analysis of the amino acid variability and of the mutational pressure directions in different parts of the genome between genovariants 1a1 and 1a2.The analysis of the consensus amino acid sequences of two genovariants and the three-dimensional structure models of protein fragments was carried out. In total, two unique amino acid substitutions in the main non-structural protein NS1 of 1a2 were found (I181M and E114G), one of which E114G is close to the DNA-binding domain (OBD) responsible for attachment to the replication origin site and can affect the rate of virus replication and transcription. Three unique amino acid substitutions were found in the structural polypeptide VP of 1a2: V30L, S98N, and N533S. Two of them are located in the most immunogenic region VP1u and can contribute to the escape from immune response. The investigation of the mutational pressure direction revealed a decrease in the frequency of G to T transversions in the second reading frame of 1a2, which reflects a higher transcription rate as a result of amino acid substitution in the OBD protein.The differences revealed between the genetic variants of subgenotype 1a B19P both in the antigenic sites and in the replication and transcription system can provide an increased “fitness” for the genetic variant 1a2 and explain its predominant distribution during the incidence rise.

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