scholarly journals A Novel Isolate with Deletion inGP3Gene of Porcine Reproductive and Respiratory Syndrome Virus from Mid-Eastern China

2014 ◽  
Vol 2014 ◽  
pp. 1-11 ◽  
Author(s):  
Baochao Fan ◽  
Hai Wang ◽  
Juan Bai ◽  
Lili Zhang ◽  
Ping Jiang
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Large Scale ◽  
Eastern China ◽  
Respiratory Syndrome Virus ◽  
Pig Farm ◽  
Prrsv Strain ◽  
Full Length Genome

PRRSV strain SH1211 was isolated from the lung tissue of a piglet on a large-scale pig farm with approximately 30% morbidity and 50% mortality in mid-eastern China in 2012. The full-length genome of SH1211 was 15 313 nt in size, excluding the polyadenylated sequences, and shared 94.9% nucleotide sequence identity with the HP-PRRSV strain, JXA1. The GP2 and GP5 proteins of SH1211 shared only 91.5% and 85.1% amino acid sequence identities with those of the JXA1, respectively. A deletion at amino acid positions 68 and 69 was identified in the GP3 protein of SH1211, compared with the GP3 of Type-2 PRRSV isolates. A phylogenetic tree based on the nucleotide sequence of the complete genome showed that SH1211 is the most closely related to other HP-PRRSV strains isolated in China. However, phylogenetic analysis based on the GP2 and GP5 proteins showed that SH1211 is the most closely related to the QYYZ strain. A recombination analysis indicated that SH1211 might have been generated through recombination events between the JXA1 and QYYZ in which the GP2 and GP5 coding sequences were exchanged. Thus, SH1211 is a novel PRRSV strain with significant variation. Our analysis of SH1211 provides insight into the role of genetic variation in the antigenicity of PRRSVs in China.

scholarly journals Complete Genome Sequence of a Recombinant Porcine Reproductive and Respiratory Syndrome Virus Strain from Two Genotype 1 Modified Live Virus Vaccine Strains

2017 ◽  
Vol 5 (22) ◽  
Author(s):  
Patricia Renson ◽  
Fabrice Touzain ◽  
Arnaud Lebret ◽  
Mireille Le Dimna ◽  
Hélène Quenault ◽  
...  
Keyword(s):  
Genome Sequence ◽  
Virus Vaccine ◽  
Complete Genome Sequence ◽  
Complete Genome ◽  
Respiratory Syndrome Virus ◽  
Genotype 1 ◽  
Live Virus ◽  
Live Virus Vaccine ◽  
Pig Farm ◽  
Prrsv Strain

ABSTRACT This paper provides information on the complete genome sequence of a porcine reproductive and respiratory syndrome virus (PRRSV) strain isolated on a French pig farm which was identified as a recombinant strain from two commercial modified live virus vaccine strains of genotype 1 (VP-046BIS and DV strains).

The nucleotide sequence of herpes simplex virus type 2 (333) glycoprotein gB2 and analysis of predicted antigenic sites

1987 ◽  
Vol 33 (10) ◽  
pp. 879-887 ◽  
Author(s):  
John C. Zwaagstra ◽  
Wai-Choi Leung
Keyword(s):  
Amino Acids ◽  
Herpes Simplex Virus ◽  
Amino Acid ◽  
Herpes Simplex ◽  
Nucleotide Sequence ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Extracellular Domain ◽  
Simplex Virus

The gene coding for glycoprotein B2 (gB2) of herpes simplex virus type 2 (HSV-2) strain 333 was mapped and its nucleotide sequence determined. Open reading frame analysis deduced a polypeptide consisting of 902 amino acids and having close homology to gB1 of HSV type 1. Several predicted features of gB2 are consistent with a membrane-bound glycoprotein, i.e., a signal peptide sequence, a hydrophilic extracellular domain containing possible N-linked glycosylation sites, a hydrophobic membrane spanning sequence, and a cytoplasmic domain. Computer analysis on hydrophilicity, accessibility, and flexibility of the gB2 amino acid sequence, produced a composite surface value plot. At least nine major antigenic regions were predicted on the extracellular domain. The amino acids between residues 59–74, 127–139, 199–205, 460–476, and 580–594 exhibited the highest surface values. Comparison of the primary sequence with gB1 revealed localized regions showing amino acid diversity. Several of these locations correspond to major antigenic regions. Chou and Fasman analyses indicated that the amino acid substitutions, between positions 57–66, 461–472, and 473–481, induced changes in the secondary structure of gB. These sites could represent site-specific epitopes in the gB polypeptide.

scholarly journals Mutational Scan of the Human Immunodeficiency Virus Type 2 Integrase Protein

1998 ◽  
Vol 72 (5) ◽  
pp. 3916-3924 ◽  
Author(s):  
Fusinita M. I. van den Ent ◽  
Arnold Vos ◽  
Ronald H. A. Plasterk
Keyword(s):  
Amino Acids ◽  
Human Immunodeficiency Virus ◽  
Amino Acid ◽  
Cleavage Reaction ◽  
Viral Dna ◽  
Dna Integration ◽  
Immunodeficiency Virus

ABSTRACT Retroviral integrase (IN) cleaves linear viral DNA specifically near the ends of the DNA (cleavage reaction) and subsequently couples the processed ends to phosphates in the target DNA (integration reaction). In vitro, IN catalyzes the disintegration reaction, which is the reverse of the integration reaction. Ideally, we would like to test the role of each amino acid in the IN protein. We mutagenized human immunodeficiency virus type 2 IN in a random way using PCR mutagenesis and generated a set of mutants in which 35% of all residues were substituted. Mutant proteins were tested for in vitro activity, e.g., site-specific cleavage of viral DNA, integration, and disintegration. Changes in 61 of the 90 proteins investigated showed no phenotypic effect. Substitutions that changed the choice of nucleophile in the cleavage reaction were found. These clustered around the active-site residues Asp-116 and Glu-152. We also found alterations of amino acids that affected cleavage and integration differentially. In addition, we analyzed the disintegration activity of the proteins and found substitutions of amino acids close to the dimer interface that enhanced intermolecular disintegration activity, whereas other catalytic activities were present at wild-type levels. This study shows the feasibility of investigating the role of virtually any amino acid in a protein the size of IN.

Variations in the major envelope glycoprotein GP5 of Czech strains of porcine reproductive and respiratory syndrome virus

2000 ◽  
Vol 81 (10) ◽  
pp. 2497-2502 ◽  
Author(s):  
Stanislav Indik ◽  
Lubomír Valíček ◽  
Dieter Klein ◽  
Jana Klánová
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Phylogenetic Tree ◽  
Envelope Glycoprotein ◽  
Point Mutations ◽  
Nucleotide Sequences ◽  
Respiratory Syndrome Virus

The major envelope glycoprotein genes (ORF5) of seven Czech isolates of porcine reproductive and respiratory syndrome virus (PRRSV) were amplified and their nucleotide sequences were determined. ORF5 displayed nucleotide and amino acid identities of 87·5–100% and 87·6–100%, respectively, among the isolates. In a phylogenetic tree, all European isolates were grouped in a genotype distinct from that of reference American strains (VR-2332, IAF-Klop). Among the European isolates, two different clades were identified. Two Czech isolates (V-501 and V-503) and Italian strain PRRSV 2156 fell into one clade. The remaining European strains comprised the second clade. Surprisingly, two separately clustered strains (V-501 and V-516) were isolated from the same herd. Additionally, the possible effect of in vitro cultivation on the nucleotide sequence was analysed. Nine point mutations in the ORF5 region resulted from 152 in vitro passages of the V-502 isolate in MARC-145 cells.

scholarly journals The 30-Amino-Acid Deletion in the Nsp2 of Highly Pathogenic Porcine Reproductive and Respiratory Syndrome Virus Emerging in China Is Not Related to Its Virulence

2009 ◽  
Vol 83 (10) ◽  
pp. 5156-5167 ◽  
Author(s):  
Lei Zhou ◽  
Jialong Zhang ◽  
Jingwen Zeng ◽  
Shuoyan Yin ◽  
Yanhua Li ◽  
...  
Keyword(s):  
Amino Acid ◽  
Parental Virus ◽  
Respiratory Syndrome Virus ◽  
Cdna Clones ◽  
Coding Region ◽  
Amino Acid Deletion ◽  
Highly Pathogenic ◽  
Specific Pathogen ◽  
Prrsv Strain ◽  
Highly Pathogenic Prrsv

ABSTRACT During the past 2 years, an atypical clinical outbreak, caused by a highly pathogenic porcine reproductive and respiratory syndrome virus (PRRSV) with a unique 30-amino-acid deletion in its Nsp2-coding region, was pandemic in China. In this study, we generated four full-length infectious cDNA clones: a clone of the highly virulent PRRSV strain JXwn06 (pWSK-JXwn), a clone of the low-virulence PRRSV strain HB-1/3.9 (pWSK-HB-1/3.9), a chimeric clone in which the Nsp2 region containing the 30-amino-acid deletion was replaced by the corresponding region of the low-virulence PRRSV strain HB-1/3.9 (pWSK-JXwn-HB1nsp2), and a mutated HB-1/3.9 clone with the same deletion in Nsp2 as JXwn06 (pWSK-HB1-ND30). We also investigated the pathogenicities of the rescued viruses (designated RvJXwn, RvJXwn-HB1nsp2, RvHB-1/3.9, and RvHB1-ND30, respectively) in specific-pathogen-free piglets in order to determine the role of the 30-amino-acid deletion in the virulence of the highly pathogenic PRRSV. All the rescued viruses could replicate stably in MARC-145 cells. Our findings indicated that RvJXwn-HB1nsp2 retained high virulence for piglets, like RvJXwn and the parental virus JXwn06, although the survival time of piglets infected with RvJXwn-HB1nsp2 was obviously prolonged. RvHB1-ND30 exhibited low virulence for piglets, like RvHB-1/3.9 and the parental virus HB-1/3.9. Therefore, we conclude that the 30-amino-acid deletion is not related to the virulence of the highly pathogenic PRRSV emerging in China.

scholarly journals Two Residues in NSP9 Contribute to the Enhanced Replication and Pathogenicity of Highly Pathogenic Porcine Reproductive and Respiratory Syndrome Virus

2018 ◽  
Vol 92 (7) ◽  
Author(s):  
Kuan Zhao ◽  
Jia-Cong Gao ◽  
Jun-Yao Xiong ◽  
Jin-Chao Guo ◽  
Yong-Bo Yang ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Molecular Mechanisms ◽  
Nonstructural Protein ◽  
Respiratory Syndrome Virus ◽  
Replication Capacity ◽  
Cdna Clones ◽  
Highly Pathogenic ◽  
Replication Efficiency ◽  
Prrsv Strain

ABSTRACT Highly pathogenic porcine reproductive and respiratory syndrome virus (HP-PRRSV) possesses greater replicative capacity and pathogenicity than classical PRRSV. However, the factors that lead to enhanced replication and pathogenicity remain unclear. In our study, an alignment of all available full-length sequences of North American-type PRRSVs ( n = 204) revealed two consistent amino acid mutations that differed between HP-PRRSV and classical PRRSV and were located at positions 519 and 544 in nonstructural protein 9. Next, a series of mutant viruses with either single or double amino acid replacements were generated from HP-PRRSV HuN4 and classical PRRSV CH-1a infectious cDNA clones. Deletion of either of the amino acids led to a complete loss of virus viability. In both Marc-145 and porcine alveolar macrophages, the replicative efficiencies of mutant viruses based on HuN4 were reduced compared to the parent, whereas the replication level of CH-1a-derived mutant viruses was increased. Plaque growth assays showed clear differences between mutant and parental viruses. In infected piglets, the pathogenicity of HuN4-derived mutant viruses, assessed through clinical symptoms, viral load in sera, histopathology examination, and thymus atrophy, was reduced. Our results indicate that the amino acids at positions 519 and 544 in NSP9 are involved in the replication efficiency of HP-PRRSV and contribute to enhanced pathogenicity. This study is the first to identify specific amino acids involved in PRRSV replication or pathogenicity. These findings will contribute to understanding the molecular mechanisms of PRRSV replication and pathogenicity, leading to better therapeutic and prognostic options to combat the virus. IMPORTANCE Porcine reproductive and respiratory syndrome (PRRS), caused by porcine reproductive and respiratory syndrome virus (PRRSV), is a significant threat to the global pig industry. Highly pathogenic PRRSV (HP-PRRSV) first emerged in China in 2006 and has subsequently spread across Asia, causing considerable damage to local economies. HP-PRRSV strains possess a greater replication capacity and higher pathogenicity than classical PRRSV strains, although the mechanisms that underlie these characteristics are unclear. In the present study, we identified two mutations in HP-PRRSV strains that distinguish them from classical PRRSV strains. Further experiments that swapped the two mutations in an HP-PRRSV strain and a classical PRRSV strain demonstrated that they are involved in the replication efficiency of the virus and its virulence. Our findings have important implications for understanding the molecular mechanisms of PRRSV replication and pathogenicity and also provide new avenues of research for the study of other viruses.

scholarly journals Lkb1 suppresses amino acid-driven gluconeogenesis in the liver

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Pierre-Alexandre Just ◽  
Sara Charawi ◽  
Raphaël G. P. Denis ◽  
Mathilde Savall ◽  
Massiré Traore ◽  
...  
Keyword(s):  
Amino Acid ◽  
Glucose Production ◽  
Whole Body ◽  
Postprandial Period ◽  
Key Factor ◽  
Liver Kinase B1 ◽  
Whole Body Metabolism ◽  
Specific Deletion

AbstractExcessive glucose production by the liver is a key factor in the hyperglycemia observed in type 2 diabetes mellitus (T2DM). Here, we highlight a novel role of liver kinase B1 (Lkb1) in this regulation. We show that mice with a hepatocyte-specific deletion of Lkb1 have higher levels of hepatic amino acid catabolism, driving gluconeogenesis. This effect is observed during both fasting and the postprandial period, identifying Lkb1 as a critical suppressor of postprandial hepatic gluconeogenesis. Hepatic Lkb1 deletion is associated with major changes in whole-body metabolism, leading to a lower lean body mass and, in the longer term, sarcopenia and cachexia, as a consequence of the diversion of amino acids to liver metabolism at the expense of muscle. Using genetic, proteomic and pharmacological approaches, we identify the aminotransferases and specifically Agxt as effectors of the suppressor function of Lkb1 in amino acid-driven gluconeogenesis.

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