Detection and molecular characterization of porcine enterovirus G15 and teschovirus from India

2020 ◽  
Vol 78 (5) ◽  
Author(s):  
Pradeep Mahadev Sawant ◽  
Nitin Atre ◽  
Abhijeet Kulkarni ◽  
Varanasi Gopalkrishna
Keyword(s):  
Amino Acid ◽  
Complete Genome ◽  
Prototype Strain ◽  
Western India ◽  
Vp1 Gene ◽  
Reading Frame ◽  
Porcine Enterovirus ◽  
Geographical Regions ◽  
Porcine Teschovirus

ABSTRACT Porcine enterovirus G (EV-G) and teschovirus (PTV) generally cause asymptomatic infections. Although both viruses have been reported from various countries, they are rarely detected from India. To detect these viruses in Western India, fecal samples (n = 26) of diarrheic piglets aged below three months from private pig farms near Pune (Maharashtra) were collected. The samples were screened by reverse transcription-polymerase chain reaction using conserved enterovirus specific primers from 5′ untranslated region. For genetic characterization of detected EV-G strain, nearly complete genome, and for PTV, partial VP1 gene were sequenced. EV-G strain showed the highest identity in a VP1 gene at nucleotide (78.61%) and amino acid (88.65%) level with EV-G15, prototype strain. However, its complete genome was homologous with the nucleotide (78.38% identity) and amino acid (91.24% identity) level to Ishi-Ka2 strain (LC316832), unassigned EV-G genotype detected from Japan. The nearly complete genome of EV-G15 consisted of 7398 nucleotides excluding the poly(A) tail and has an open reading frame that encodes a 2170 amino acid polyprotein. Genetic analysis of the partial VP1 gene of teschovirus identified porcine teschovirus 4 (PTV-4) and putative PTV-17 genotype. To the best of our knowledge, this is the first report on nearly full genome characterization of EV-G15, and detection of PTV-4 and putative PTV-17 genotypes from India. Further, detection and characterization of porcine enteroviruses are needed for a comprehensive understanding of their genetic diversity and their association with symptomatic infections from other geographical regions of India.

scholarly journals Identification and complete genome characterization of a novel picornavirus in turkey (Meleagris gallopavo)

2012 ◽  
Vol 93 (10) ◽  
pp. 2171-2182 ◽  
Author(s):  
Ákos Boros ◽  
Csaba Nemes ◽  
Péter Pankovics ◽  
Beatrix Kapusinszky ◽  
Eric Delwart ◽  
...  
Keyword(s):  
Amino Acid ◽  
Complete Genome ◽  
Bird Species ◽  
Entry Site ◽  
Pathogenic Potential ◽  
Genome Characterization ◽  
Genome Region ◽  
Faecal Samples ◽  
The Usa

Members of the family Picornaviridae are important pathogens of humans and animals, although compared with the thousands of known bird species (>10 000), only a few (n = 11) picornaviruses have been identified from avian sources. This study reports the metagenomic detection and complete genome characterization of a novel turkey picornavirus from faecal samples collected from eight turkey farms in Hungary. Using RT-PCR, both healthy (two of three) and affected (seven of eight) commercial turkeys with enteric and/or stunting syndrome were shown to be shedding viruses in seven (88 %) of the eight farms. The viral genome sequence (turkey/M176/2011/HUN; GenBank accession no. JQ691613) shows a high degree of amino acid sequence identity (96 %) to the partial P3 genome region of a picornavirus reported recently in turkey and chickens from the USA and probably belongs to the same species. In the P1 and P2 regions, turkey/M176/2011/HUN is related most closely to, but distinct from, the kobuviruses and turdivirus 1. Complete genome analysis revealed the presence of characteristic picornaviral amino acid motifs, a potential type II-like 5′ UTR internal ribosome entry site (first identified among avian-origin picornaviruses) and a conserved, 48 nt long ‘barbell-like’ structure found at the 3′ UTR of turkey/M176/2011/HUN and members of the picornavirus genera Avihepatovirus and Kobuvirus. The general presence of turkey picornavirus – a novel picornavirus species – in faecal samples from healthy and affected turkeys in Hungary and in the USA suggests the worldwide occurrence and endemic circulation of this virus in turkey farms. Further studies are needed to investigate the aetiological role and pathogenic potential of this picornavirus in food animals.

scholarly journals Characterization of hepatitis B virus genotypes among Yucpa Indians in Venezuela

2001 ◽  
Vol 82 (2) ◽  
pp. 359-365 ◽  
Author(s):  
Tatsunori Nakano ◽  
Ling Lu ◽  
Xiaolei Hu ◽  
Masashi Mizokami ◽  
Etsuro Orito ◽  
...  
Keyword(s):  
Hepatitis B Virus ◽  
Hepatitis B ◽  
Complete Genome ◽  
Deletion Mutants ◽  
Reading Frame ◽  
B Virus ◽  
Virus Genotypes ◽  
Core Reading ◽  
Genotype F

The complete genome sequences of hepatitis B virus (HBV) from 12 HBV-infected Yucpa Indians of Venezuela, a group with highly endemic HBV, were amplified and sequenced. The 12 isolates were closely related to each other, with 98·6–100% nucleotide identity. A phylogenetic tree based on the complete genome indicated clearly that they were genotype F. Three individuals had evidence of infection with two different HBV deletion mutants. In two individuals, a three amino acid deletion was identified just prior to the ‘a’ determinant loop of the S region. A third individual was infected with virus that contained a complete core reading frame and a population that contained a deletion in the middle of the core region. These results indicate that genotype F HBV is present in the Venezuelan Yucpa Amerindians and the complete genome sequence allowed the identification of two unique deletion mutants in a limited set of samples.

scholarly journals Characterization of the ToxB Gene from Pyrenophora tritici-repentis

2001 ◽  
Vol 14 (5) ◽  
pp. 675-677 ◽  
Author(s):  
J. Patrick Martinez ◽  
Sean A. Ottum ◽  
Shaukat Ali ◽  
Leonard J. Francl ◽  
Lynda M. Ciuffetti
Keyword(s):  
Amino Acid ◽  
Pichia Pastoris ◽  
Heterologous Expression ◽  
North Dakota ◽  
Signal Peptide ◽  
Open Reading Frame ◽  
Reading Frame ◽  
Pyrenophora Tritici Repentis ◽  
Putative Signal Peptide

The ToxB gene was cloned and characterized from a race 5 isolate of Pyrenophora tritici-repentis from North Dakota. ToxB contains a 261-bp open reading frame that encodes a 23 amino acid putative signal peptide and a 64 amino acid host-selective toxin, Ptr ToxB. Analysis of Ptr ToxB from heterologous expression in Pichia pastoris confirms that ToxB encodes a host-selective toxin.

Gene Cloning, Nucleotide Sequencing, and Purification and Characterization of the Low-Specificityl-Threonine Aldolase from Pseudomonas sp. Strain NCIMB 10558

1998 ◽  
Vol 64 (2) ◽  
pp. 549-554 ◽  
Author(s):  
Ji-Quan Liu ◽  
Saeko Ito ◽  
Tohru Dairi ◽  
Nobuya Itoh ◽  
Michihiko Kataoka ◽  
...  
Keyword(s):  
Amino Acid ◽  
Significant Loss ◽  
Site Directed Mutagenesis ◽  
Nucleotide Sequencing ◽  
Predicted Amino Acid Sequence ◽  
Amino Acid Residues ◽  
Purification And Characterization ◽  
Reading Frame ◽  
Threonine Aldolase

ABSTRACT A low-specificity l-threonine aldolase (l-TA) gene from Pseudomonas sp. strain NCIMB 10558 was cloned and sequenced. The gene contains an open reading frame consisting of 1,041 nucleotides corresponding to 346 amino acid residues. The gene was overexpressed in Escherichia colicells, and the recombinant enzyme was purified and characterized. The enzyme, requiring pyridoxal 5′-phosphate as a coenzyme, is strictlyl specific at the α position, whereas it cannot distinguish between threo and erythro forms at the β position. In addition to threonine, the enzyme also acts on various other l-β-hydroxy-α-amino acids, includingl-β-3,4-dihydroxyphenylserine,l-β-3,4-methylenedioxyphenylserine, andl-β-phenylserine. The predicted amino acid sequence displayed less than 20% identity with those of low-specificityl-TA from Saccharomyces cerevisiae,l-allo-threonine aldolase from Aeromonas jandaei, and four relevant hypothetical proteins from other microorganisms. However, lysine 207 of low-specificity l-TA from Pseudomonas sp. strain NCIMB 10558 was found to be completely conserved in these proteins. Site-directed mutagenesis experiments showed that substitution of Lys207 with Ala or Arg resulted in a significant loss of enzyme activity, with the corresponding disappearance of the absorption maximum at 420 nm. Thus, Lys207 of thel-TA probably functions as an essential catalytic residue, forming an internal Schiff base with the pyridoxal 5′-phosphate of the enzyme to catalyze the reversible aldol reaction.

scholarly journals Genomic Characterization of Severe Acute Respiratory Syndrome-Related Coronavirus in European Bats and Classification of Coronaviruses Based on Partial RNA-Dependent RNA Polymerase Gene Sequences

2010 ◽  
Vol 84 (21) ◽  
pp. 11336-11349 ◽  
Author(s):  
Jan Felix Drexler ◽  
Florian Gloza-Rausch ◽  
Jörg Glende ◽  
Victor Max Corman ◽  
Doreen Muth ◽  
...  
Keyword(s):  
Amino Acid ◽  
Severe Acute Respiratory Syndrome ◽  
Surface Expression ◽  
Emerging Viruses ◽  
Reading Frame ◽  
High Frequencies ◽  
Nyctalus Leisleri ◽  
Genomic Characterization

ABSTRACT Bats may host emerging viruses, including coronaviruses (CoV). We conducted an evaluation of CoV in rhinolophid and vespertilionid bat species common in Europe. Rhinolophids carried severe acute respiratory syndrome (SARS)-related CoV at high frequencies and concentrations (26% of animals are positive; up to 2.4 × 108 copies per gram of feces), as well as two Alphacoronavirus clades, one novel and one related to the HKU2 clade. All three clades present in Miniopterus bats in China (HKU7, HKU8, and 1A related) were also present in European Miniopterus bats. An additional novel Alphacoronavirus clade (bat CoV [BtCoV]/BNM98-30) was detected in Nyctalus leisleri. A CoV grouping criterion was developed by comparing amino acid identities across an 816-bp fragment of the RNA-dependent RNA polymerases (RdRp) of all accepted mammalian CoV species (RdRp-based grouping units [RGU]). Criteria for defining separate RGU in mammalian CoV were a >4.8% amino acid distance for alphacoronaviruses and a >6.3% distance for betacoronaviruses. All the above-mentioned novel clades represented independent RGU. Strict associations between CoV RGU and host bat genera were confirmed for six independent RGU represented simultaneously in China and Europe. A SARS-related virus (BtCoV/BM48-31/Bulgaria/2008) from a Rhinolophus blasii (Rhi bla) bat was fully sequenced. It is predicted that proteins 3b and 6 were highly divergent from those proteins in all known SARS-related CoV. Open reading frame 8 (ORF8) was surprisingly absent. Surface expression of spike and staining with sera of SARS survivors suggested low antigenic overlap with SARS CoV. However, the receptor binding domain of SARS CoV showed higher similarity with that of BtCoV/BM48-31/Bulgaria/2008 than with that of any Chinese bat-borne CoV. Critical spike domains 472 and 487 were identical and similar, respectively. This study underlines the importance of assessments of the zoonotic potential of widely distributed bat-borne CoV.

scholarly journals Purification and Characterization of the Coniferyl Aldehyde Dehydrogenase from Pseudomonas sp. Strain HR199 and Molecular Characterization of the Gene

1998 ◽  
Vol 180 (17) ◽  
pp. 4387-4391 ◽  
Author(s):  
Sandra Achterholt ◽  
Horst Priefert ◽  
Alexander Steinbüchel
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Ferulic Acid ◽  
Aldehyde Dehydrogenase ◽  
Genomic Library ◽  
Aromatic Aldehydes ◽  
Amino Acid Identity ◽  
Reading Frame ◽  
Relative Molecular Weight

ABSTRACT The coniferyl aldehyde dehydrogenase (CALDH) ofPseudomonas sp. strain HR199 (DSM7063), which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid and which is induced during growth with eugenol as the carbon source, was purified and characterized. The native protein exhibited an apparent molecular mass of 86,000 ± 5,000 Da, and the subunit mass was 49.5 ± 2.5 kDa, indicating an α2 structure of the native enzyme. The optimal oxidation of coniferyl aldehyde to ferulic acid was obtained at a pH of 8.8 and a temperature of 26°C. The Km values for coniferyl aldehyde and NAD+ were about 7 to 12 μM and 334 μM, respectively. The enzyme also accepted other aromatic aldehydes as substrates, whereas aliphatic aldehydes were not accepted. The NH2-terminal amino acid sequence of CALDH was determined in order to clone the encoding gene (calB). The corresponding nucleotide sequence was localized on a 9.4-kbp EcoRI fragment (E94), which was subcloned from a Pseudomonas sp. strain HR199 genomic library in the cosmid pVK100. The partial sequencing of this fragment revealed an open reading frame of 1,446 bp encoding a protein with a relative molecular weight of 51,822. The deduced amino acid sequence, which is reported for the first time for a structural gene of a CALDH, exhibited up to 38.5% amino acid identity (60% similarity) to NAD+-dependent aldehyde dehydrogenases from different sources.

scholarly journals Complete Genome Sequence of a Novel Human Betapapillomavirus Isolated from a Skin Sample

2017 ◽  
Vol 5 (13) ◽  
Author(s):  
Sankhadeep Dutta ◽  
Alexis Robitaille ◽  
Dana E. Rollison ◽  
Massimo Tommasino ◽  
Tarik Gheit
Keyword(s):  
Human Papillomavirus ◽  
Genome Sequence ◽  
Complete Genome Sequence ◽  
Complete Genome ◽  
Genetic Characterization ◽  
Open Reading Frame ◽  
Skin Sample ◽  
Reading Frame ◽  
Beta 2

ABSTRACT We report the genetic characterization of a new papillomavirus (HPV_MTS1) isolated and fully cloned from a skin swab. The L1 open reading frame of HPV_MTS1 was 85% identical to its closest human papillomavirus (HPV) type 80, which belongs to the species beta-2 of the genus Betapapillomavirus, hence qualifying it as a new HPV type.

scholarly journals Characterization of a DivergentvanD-Type Resistance Element from the First Glycopeptide-Resistant Strain of Enterococcus faeciumIsolated in Brazil

2000 ◽  
Vol 44 (12) ◽  
pp. 3444-3446 ◽  
Author(s):  
Libera M. Dalla Costa ◽  
Peter E. Reynolds ◽  
Helena A. P. H. M. Souza ◽  
Dilair C. Souza ◽  
Marie-France I. Palepou ◽  
...  
Keyword(s):  
Amino Acid ◽  
Resistant Strain ◽  
Enterococcus Faecium ◽  
Amino Acid Identity ◽  
Open Reading Frame ◽  
Glycopeptide Resistance ◽  
Reading Frame ◽  
Acid Identity ◽  
Resistance Phenotype

ABSTRACT Enterococcus faecium 10/96A from Brazil was resistant to vancomycin (MIC, 256 μg/ml) but gave no amplification products with primers specific for known van genotypes. A 2,368-bp fragment of a van cluster contained one open reading frame encoding a peptide with 83% amino acid identity to VanHD, and a second encoding a d-alanine-d-lactate ligase with 83 to 85% identity to VanD. The divergent glycopeptide resistance phenotype was designated VanD4.

scholarly journals Characterization of an Immunogenic Outer Membrane Autotransporter Protein, Arp, of Bartonella henselae

2007 ◽  
Vol 75 (11) ◽  
pp. 5255-5263 ◽  
Author(s):  
Christine M. Litwin ◽  
Mindy L. Rawlins ◽  
Erica M. Swenson
Keyword(s):  
Amino Acid ◽  
Molecular Mass ◽  
Outer Membrane ◽  
Dna Sequences ◽  
Bartonella Henselae ◽  
Cross Reactivity ◽  
Passenger Domain ◽  
Calculated Molecular Mass ◽  
Reading Frame

ABSTRACT Bartonella henselae is a recently recognized pathogenic bacterium associated with cat scratch disease, bacillary angiomatosis, and bacillary peliosis. This study describes the cloning, sequencing, and characterization of an antigenic autotransporter gene from B. henselae. A cloned 6.0-kb BclI-EcoRI DNA fragment expresses a 120-kDa B. henselae protein immunoreactive with 21.2% of sera from patients positive for B. henselae immunoglobulin G antibodies by indirect immunofluorescence, with 97.3% specificity and no cross-reactivity with antibodies against various other organisms. DNA sequencing of the clone revealed one open reading frame of 4,320 bp with a deduced amino acid sequence that shows homology to the family of autotransporters. The autotransporters are a group of proteins that mediate their own export through the outer membrane and consist of a passenger region, the α-domain, and an outer membrane transporter region, the β-domain. The passenger domain shows homology to a family of pertactin-like adhesion proteins and contains seven, nearly identical 48-amino-acid repeats not found in any other bacterial or Bartonella DNA sequences. The passenger α-domain has a calculated molecular mass of 117 kDa, and the transporter β-domain has a calculated molecular mass of 36 kDa. The clone expresses a 120-kDa protein and a protein that migrates at approximately 38 kDa exclusively in the outer membrane protein fraction, suggesting that the 120-kDa passenger protein remains associated with the outer membrane after cleavage from the 36-kDa transporter.

scholarly journals Complete genome sequence analysis of a novel bunyavirus isolated from Paris polyphylla var. yunnanensis

2021 ◽  
Author(s):  
Zeli Chen ◽  
Rex Frimpong Anane ◽  
Zhe Wang ◽  
Like Gao ◽  
Lu Chen ◽  
...  
Keyword(s):  
Amino Acid ◽  
Genome Sequence ◽  
Complete Genome Sequence ◽  
Complete Genome ◽  
Rna Virus ◽  
Amino Acid Sequences ◽  
Reading Frame ◽  
Leaf Chlorosis ◽  
Paris Polyphylla ◽  
Complete Genome Sequence Analysis

Abstract A novel negative-stranded (ns) RNA virus tentatively named “Yunnan manyleaf paris rhizome negative-stranded virus 1” (YMPrNSV1), was isolated from a Paris polyphylla var. yunnanensis plant exhibiting leaf chlorosis and mosaic symptoms in Yunnan. Its complete genome sequence was determined using Illumina and Sanger sequencing. The genomes composed of three RNA segments (L, M and S) with each one containing a single open reading frame. Based on sequence identity and the presence of typical bunya-like domains/motifs, the proteins encoded by YMPrNSV1 were predicted to be: RNA-dependent RNA polymerase (RdRp), putative movement protein (MP), and nucleocapsid protein (NP). Sequence comparison analyses showed that the RdRp, MP and NP of YMPrNSV1 are highly similar to those of watermelon crinkle leaf-associated virus 2 (WCLaV-2), with 69.1%, 50.4% and 60.9% amino acid sequence identities respectively. Phylogenetic analysis based on deduced amino acid sequences of RdRp and NP suggested that YMPrNSV1 clustered with coguviruses in a clade, and that WCLaV-2 is the known closely related species to YMPrNSV1. Base on the above results, YMPrNSV1 should be regarded as a new member of genera Coguvirus, within the family Phenuiviridae.

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