Sequence analysis of three non structural proteins of a porcine group C (Cowden strain) rotavirus

1993 ◽  
Vol 130 (1-2) ◽  
pp. 85-92 ◽  
Author(s):  
M. Bremont ◽  
D. Chabanne-Vautherot ◽  
J. Cohen
Keyword(s):  
Sequence Analysis ◽  
Structural Proteins ◽  
Cowden Strain

Variability of non-structural proteins of equine arteritis virus during persistent infection of the stallion

2015 ◽  
Vol 18 (2) ◽  
pp. 255-259 ◽  
Author(s):  
W. Socha ◽  
J. Rola ◽  
J.F. Żmudziński
Keyword(s):  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Identity ◽  
Equine Arteritis Virus ◽  
The Other ◽  
Structural Proteins ◽  
Amino Acid Substitutions ◽  
Synonymous Substitutions ◽  
Acid Identity ◽  
Synonymous Mutations

AbstractThe genetic stability of ORF1a encoding non-structural proteins nsp1, nsp2, nsp3 and nsp4 of equine arteritis virus (EAV) has been analysed for nearly seven years in a persistently infected stallion of the Malopolska breed. Between November 2004 and June 2011, 11 semen samples were collected. Viral RNA extracted from semen of this carrier stallion was amplified, sequenced and compared with the sequences of the other known strains of EAV. Sequence analysis of ORF1a showed 84 synonymous and 16 non-synonymous mutations. The most variable part of ORF1a was the region encoding nsp2 protein with 13 non-synonymous substitutions. The degree of amino acid identity between isolates ranged from 98.91 to 100%. Only single non-synonymous mutations were detected in nsp1 (one substitution) and nsp4 (two substitutions). The most stable was nsp3 in which no amino acid substitutions were observed during the whole period of observation.

scholarly journals Molecular characterization of a novel adult diarrhoea rotavirus strain J19 isolated in China and its significance for the evolution and origin of group B rotaviruses

2008 ◽  
Vol 89 (10) ◽  
pp. 2622-2629 ◽  
Author(s):  
Shengjun Jiang ◽  
Shaozhong Ji ◽  
Qing Tang ◽  
Xiaoying Cui ◽  
Hongyang Yang ◽  
...  
Keyword(s):  
Phylogenetic Analysis ◽  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Complete Genome ◽  
Amino Acid Sequence Identity ◽  
Structural Proteins ◽  
Protein Sequence Analysis ◽  
Sequence Identity ◽  
Group B

The complete genome of a novel adult diarrhoea rotavirus strain J19 was cloned and sequenced using an improved single-primer sequence-independent method. The complete genome is 17 961 bp and is AU-rich (66.49 %). Northern blot analysis and genomic sequence analysis indicated that segments 1–11 encode 11 viral proteins, respectively. Protein alignments with the corresponding proteins of J19 with B219, and groups A, B and C rotaviruses, produced higher per cent sequence identities to B219. Among groups A, B and C rotaviruses, 10 proteins from group B rotaviruses exhibited slightly higher amino acid sequence identity to the J19 proteins, but proteins of J19 showed low amino acid sequence identity with groups A and C rotaviruses. Construction of unrooted phylogenetic trees using a set of known proteins and representatives of three known rotavirus groups revealed that six structural proteins were positioned close to B219 and the basal nodes of groups A, B and C lineages, although with a preferred association with group B lineages. Phylogenetic analysis of the five non-structural proteins showed a similar trend. The results of the serological analysis, protein sequence analysis and phylogenetic analysis suggested that J19 would be a novel rotavirus strain with great significance to the evolution and origin of group B rotaviruses.

scholarly journals Sequence Analysis and Amino Acid Variations of Structural Proteins Deduced From Novel Coronavirus SARS-CoV-2 Strains, Isolated in Different Countries

2020 ◽  
Author(s):  
Tarlan Mamedov ◽  
Inanc Soylu ◽  
Gunay Mammadova ◽  
Gulnara Hasanova
Keyword(s):  
Amino Acid ◽  
Sequence Analysis ◽  
Nucleocapsid Protein ◽  
Matrix Protein ◽  
Structural Proteins ◽  
Therapeutic Drug ◽  
E Proteins ◽  
Multiple Sequence ◽  
Highly Pathogenic ◽  
Novel Coronavirus

SARS-CoV-2 is a novel and highly pathogenic coronavirus, which was first diagnosed in Wuhan city, China, in 2019, and spread to 185 countries and territories, and as of April 29, 2020, more than 3.11 million cases were recorded, and more than 217,000 people were killed. Despite all worldwide efforts, there is currently no vaccine, any drugs available to protect people against deadly SARS-CoV-2 coronavirus. The world urgently needs a SARS-CoV-2 coronavirus vaccine or effective antiviral drugs to relieve the human suffering associated with the pandemic that kills thousands of people every day. The SARS-CoV-2 genome encode a non-structural proteins named as ORF1a/b, and structural proteins such as spike (S) glycoprotein, nucleocapsid protein (N), small envelop protein (E) and matrix protein (M). A number of studies have been shown that CoV spike (S) glycoprotein and nucleocapsid protein (N) could be promising targets for vaccine, antibodies and therapeutic drug development to combat with deadly, pandemic SARS-CoV-2. Purposes of the present paper is the sequence analysis and amino acid variations of structural proteins deduced from novel coronavirus SARS-CoV-2 strains, isolated in different countries. Multiple sequence alignment of S, N and E proteins from four different coronavirus species, are also described. It is expected that the data from these studies will be very useful for the the designing and development of vaccines, antibodies and therapeutic agents that can be used to combat with the highly pathogenic SARS-CoV-2 coronavirus worldwide.

Exposure of protein VP7 on the surface of bluetongue virus

1990 ◽  
Vol 48 (3) ◽  
pp. 600-601
Author(s):  
A.D. Hyatt
Keyword(s):  
Bluetongue Virus ◽  
Structural Proteins ◽  
Major Constituent ◽  
Outer Coat ◽  
Virus Particles ◽  
Antibody Recognition ◽  
The Core ◽  
The Family ◽  
Electron Microscopical ◽  
Physical Accessibility

Bluetongue virus (BTV) is the type species os the genus orbivirus in the family Reoviridae. The virus has a fibrillar outer coat containing two major structural proteins VP2 and VP5 which surround an icosahedral core. The core contains two major proteins VP3 and VP7 and three minor proteins VP1, VP4 and VP6. Recent evidence has indicated that the core comprises a neucleoprotein center which is surrounded by two protein layers; VP7, a major constituent of capsomeres comprises the outer and VP3 the inner layer of the core . Antibodies to VP7 are currently used in enzyme-linked immunosorbant assays and immuno-electron microscopical (JEM) tests for the detection of BTV. The tests involve the antibody recognition of VP7 on virus particles. In an attempt to understand how complete viruses can interact with antibodies to VP7 various antibody types and methodologies were utilized to determine the physical accessibility of the core to the external environment.

Phylogeny and taxonomy of the family Arthrodermataceae (dermatophytes) using sequence analysis of the ribosomal ITS region

1999 ◽  
Vol 37 (2) ◽  
pp. 105-114 ◽  
Author(s):  
Y. GRAser ◽  
M. EL Fari ◽  
R. Vilgalys ◽  
A. F. A. Kuijpers ◽  
G. S. DE Hoog ◽  
...  
Keyword(s):  
Sequence Analysis ◽  
Its Region ◽  
The Family
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