scholarly journals Isolation and Characterization of 2019-nCoV-like Coronavirus from Malayan Pangolins

2020 ◽  
Author(s):  
Kangpeng Xiao ◽  
Junqiong Zhai ◽  
Yaoyu Feng ◽  
Niu Zhou ◽  
Xu Zhang ◽  
...  
Keyword(s):  
Public Health ◽  
Amino Acid ◽  
Clinical Signs ◽  
Amino Acid Identity ◽  
Reservoir Host ◽  
Wildlife Trade ◽  
Amino Acid Difference ◽  
High Sequence Identity ◽  
S Protein ◽  
Isolation And Characterization

AbstractThe outbreak of 2019-nCoV in the central Chinese city of Wuhan at the end of 2019 poses unprecedent public health challenges to both China and the rest world1. The new coronavirus shares high sequence identity to SARS-CoV and a newly identified bat coronavirus2. While bats may be the reservoir host for various coronaviruses, whether 2019-nCoV has other hosts is still ambiguous. In this study, one coronavirus isolated from Malayan pangolins showed 100%, 98.2%, 96.7% and 90.4% amino acid identity with 2019-nCoV in the E, M, N and S genes, respectively. In particular, the receptor-binding domain of the S protein of the Pangolin-CoV is virtually identical to that of 2019-nCoV, with one amino acid difference. Comparison of available genomes suggests 2019-nCoV might have originated from the recombination of a Pangolin-CoV-like virus with a Bat-CoV-RaTG13-like virus. Infected pangolins showed clinical signs and histopathological changes, and the circulating antibodies reacted with the S protein of 2019-nCoV. The isolation of a coronavirus that is highly related to 2019-nCoV in the pangolins suggests that these animals have the potential to act as the intermediate host of 2019-nCoV. The newly identified coronavirus in the most-trafficked mammal could represent a continuous threat to public health if wildlife trade is not effectively controlled.

scholarly journals Mobuck virus genome sequence and phylogenetic analysis: identification of a novel Orbivirus isolated from a white-tailed deer in Missouri, USA

2014 ◽  
Vol 95 (1) ◽  
pp. 110-116 ◽  
Author(s):  
Elyse Cooper ◽  
Srivishnupriya Anbalagan ◽  
Patricia Klumper ◽  
Gail Scherba ◽  
Randy R. Simonson ◽  
...  
Keyword(s):  
Phylogenetic Analysis ◽  
Amino Acid ◽  
Clinical Signs ◽  
Amino Acid Identity ◽  
Virus Genome ◽  
The Novel ◽  
Structural Protein ◽  
Middle Point ◽  
Wide Range ◽  
Haemorrhagic Disease

The genus Orbivirus includes a diverse group of segmented dsRNA viruses that are transmitted via arthropods, have a global distribution and affect a wide range of hosts. A novel orbivirus was co-isolated with epizootic haemorrhagic disease virus (EHDV) from a white-tailed deer (Odocoileus virginianus) exhibiting clinical signs characteristic of EHDV. Using antiserum generated against EHDV, a pure isolate of the novel non-cytopathic orbivirus was obtained in Aedes albopictus cell culture. Genomic sequencing and phylogenetic analysis of predicted ORFs showed that eight of the ten ORFs were most homologous to Peruvian horse sickness virus (PHSV), with amino acid identities of 44.3–73.7 %. The remaining two ORFs, VP3 and VP5, were most similar to Middle Point orbivirus (35.9 %) and Yunnan orbivirus (59.8 %), respectively. Taxonomic classification of orbiviruses is largely based on homology of the major subcore structural protein VP2(T2), encoded by segment 2 for mobuck virus. With only 69.1 % amino acid identity to PHSV, we propose mobuck virus as the prototype of a new species of Orbivirus.

Isolation and characterization of Drosophila multidrug resistance gene homologs

1991 ◽  
Vol 11 (8) ◽  
pp. 3940-3948
Author(s):  
C T Wu ◽  
M Budding ◽  
M S Griffin ◽  
J M Croop
Keyword(s):  
Amino Acid ◽  
Cell Lines ◽  
Multidrug Resistant ◽  
Amino Acid Identity ◽  
Resistant Cell ◽  
Cross Resistance ◽  
Multidrug Resistance Gene ◽  
Isolation And Characterization ◽  
P Glycoprotein

Mammalian multidrug-resistant cell lines, selected for resistance to a single cytotoxic agent, display cross-resistance to a broad spectrum of structurally and functionally unrelated compounds. These cell lines overproduce a membrane protein, the P-glycoprotein, which is encoded by a member(s) of a multigene family, termed mdr or pgp. The amino acid sequence of the P-glycoprotein predicts an energy-dependent transport protein with homology to a large superfamily of proteins which transport a wide variety of substances. This report describes the isolation and characterization of two Drosophila homologs of the mammalian mdr gene. These homologs, located in chromosomal sections 49EF and 65A, encode proteins that share over 40% amino acid identity to the human and murine mdr P-glycoproteins. Fly strains bearing disruptions in the homolog in section 49EF have been constructed and implicate this gene in conferring colchicine resistance to the organism. This work sets the foundation for the molecular and genetic analysis of mdr homologs in Drosophila melanogaster.

LeAbsi1 gene expression regulation by various abiotic and oxidative stresses

2010 ◽  
Vol 90 (4) ◽  
pp. 435-441
Author(s):  
J. Guo ◽  
M -H. Wang
Keyword(s):  
Oxidative Stress ◽  
Amino Acid ◽  
Gene Expression Regulation ◽  
Solanum Melongena ◽  
Amino Acid Identity ◽  
Temperature Treatment ◽  
High Sequence Identity ◽  
Oxidative Stresses ◽  
Low Temperature Treatment ◽  
High Amino Acid

A full-length LeAbsi1 cDNA was isolated from the tomato (Lycopersicon esculentum L.) plant. Phylogenetic analysis was performed, based on the deduced amino acid sequence of the LeAbsi1 cDNA and revealed high amino acid identity (AAID) to unknown proteins in Solanum melongena (87% AAID) and Petunia integrifolia (80% AAID). LeAbsi1 shares high sequence identity with a zinc finger (C2H2-type) family protein from Arabidopsis (53% AAID) and the CaAbsi1 protein in Capsicum annuum (49% AAID). Expression of the LeAbsi1 gene under abiotic and oxidative stresses was investigated in this study, including exposure to the conditions of 200 mM NaCl, 200 mM mannitol, cold temperature (4°C), 100 µM abscisic acid (ABA), 10 mM hydrogen peroxide (H2O2), and 50 µMM methyl vilogen (MV). LeAbsi1 was significantly induced after a 3 h exposure to NaCl, mannitol and low temperature treatment. Its transcripts also accumulated strongly after plant hormone ABA treatment for 1 h. Moreover, LeAbsi1 was significantly induced by MV treatments after 6 h. These observations suggest that the LeAbsi1 gene plays a role in both abiotic and oxidative stress responses.Key words: Abiotic stress, LeAbsi1, tomato, oxidative stress

scholarly journals Characterization of a novel flavivirus isolated from Culex (Melanoconion) ocossa mosquitoes from Iquitos, Peru

2013 ◽  
Vol 94 (6) ◽  
pp. 1266-1272 ◽  
Author(s):  
Julio Evangelista ◽  
Cristhopher Cruz ◽  
Carolina Guevara ◽  
Helvio Astete ◽  
Cristiam Carey ◽  
...  
Keyword(s):  
Amino Acid ◽  
Mammalian Cells ◽  
Amazon Basin ◽  
Yellow Fever Virus ◽  
Amino Acid Identity ◽  
Amino Acid Sequences ◽  
Newborn Mice ◽  
Isolation And Characterization ◽  
Indirect Immunofluorescent Assay

We describe the isolation and characterization of a novel flavivirus, isolated from a pool of Culex (Melanoconion) ocossa Dyar and Knab mosquitoes collected in 2009 in an urban area of the Amazon basin city of Iquitos, Peru. Flavivirus infection was detected by indirect immunofluorescent assay of inoculated C6/36 cells using polyclonal flavivirus antibodies (St. Louis encephalitis virus, yellow fever virus and dengue virus type 1) and confirmed by RT-PCR. Based on partial sequencing of the E and NS5 gene regions, the virus isolate was most closely related to the mosquito-borne flaviviruses but divergent from known species, with less than 45 and 71 % pairwise amino acid identity in the E and NS5 gene products, respectively. Phylogenetic analysis of E and NS5 amino acid sequences demonstrated that this flavivirus grouped with mosquito-borne flaviviruses, forming a clade with Nounané virus (NOUV). Like NOUV, no replication was detected in a variety of mammalian cells (Vero-76, Vero-E6, BHK, LLCMK, MDCK, A549 and RD) or in intracerebrally inoculated newborn mice. We tentatively designate this genetically distinct flavivirus as representing a novel species, Nanay virus, after the river near where it was first detected.

scholarly journals Characterization of a novel Negevirus and a novel Bunyavirus isolated from Culex (Culex) declarator mosquitoes in Trinidad

2014 ◽  
Vol 95 (2) ◽  
pp. 481-485 ◽  
Author(s):  
Albert J. Auguste ◽  
Christine V. F. Carrington ◽  
Naomi L. Forrester ◽  
Vsevolod L. Popov ◽  
Hilda Guzman ◽  
...  
Keyword(s):  
Amino Acid ◽  
Cote D'ivoire ◽  
Côte D’Ivoire ◽  
Amino Acid Identity ◽  
Cote D’Ivoire ◽  
Newborn Mice ◽  
Isolation And Characterization ◽  
Côte D'ivoire ◽  
Phlebotomine Sandflies

Pools of mosquitoes were tested for insect-specific viruses using cytopathic effect (CPE) assays on Aedes albopictus (C6/36) cells. Illumina sequencing of RNA from pool TR7094, which produced extensive CPE 2 days post-infection, yielded the complete genome sequences of a previously unknown Bunyavirus, designated Cumuto virus (CUMV), and a second virus designated Wallerfield virus (WALV). WALV shared highest amino acid identity (60.1 %) with Dezidougou virus from Côte d’Ivoire, a positive-sense, single-strand RNA, insect-specific virus belonging to the newly proposed genus Negevirus associated with mosquitoes and phlebotomine sandflies. The S, M and L segments of CUMV were most closely related to those of Gouleako virus, also from Côte d’Ivoire (amino acid identities of 36 %, 38 % and 54 % respectively). Neither virus produced CPE on vertebrate cells, or illness in newborn mice. Isolation and characterization of these viruses increase our knowledge of the geographical distribution, diversity and host range of mosquito-specific bunyaviruses and negeviruses.

scholarly journals Complete Genomic Sequencing Shows that Polioviruses and Members of Human Enterovirus Species C Are Closely Related in the Noncapsid Coding Region

2003 ◽  
Vol 77 (16) ◽  
pp. 8973-8984 ◽  
Author(s):  
Betty Brown ◽  
M. Steven Oberste ◽  
Kaija Maher ◽  
Mark A. Pallansch
Keyword(s):  
Amino Acid ◽  
Phylogenetic Trees ◽  
Amino Acid Identity ◽  
Human Enterovirus ◽  
Amino Acid Difference ◽  
Coding Region ◽  
Capsid Region ◽  
Capsid Sequence ◽  
Close Relationship ◽  
Complete Sequences

ABSTRACT The 65 human enterovirus serotypes are currently classified into five species: Poliovirus (3 serotypes), Human enterovirus A (HEV-A) (12 serotypes), HEV-B (37 serotypes), HEV-C (11 serotypes), and HEV-D (2 serotypes). Coxsackie A virus (CAV) serotypes 1, 11, 13, 15, 17, 18, 19, 20, 21, 22, and 24 constitute HEV-C. We have determined the complete genome sequences for the remaining nine HEV-C serotypes and compared them with the complete sequences of CAV21, CAV24, and the polioviruses. The viruses were most diverse in the capsid region (4 to 36% amino acid difference). A high degree of capsid sequence conservation (96% amino acid identity) suggests that CAV15 and CAV18 should be classified as strains of CAV11 and CAV13, respectively. In the 3CD region, CAV1, CAV19, and CAV22 differed from one another by only 1.2 to 1.4% and CAV11, CAV13, CAV17, CAV20, CAV21, CAV24, and the polioviruses differed from one another by only 1.2 to 3.6%. The two groups, however, differed from one another by 14.6 to 16.2%. The polioviruses as a group were monophyletic only in the capsid region. Only one group of serotypes (CAV1, CAV19, and CAV22) was consistently monophyletic in multiple genome regions. Incongruities among phylogenetic trees based on different genome regions strongly suggest that recombination has occurred between the polioviruses, CAV11, CAV13, CAV17, and CAV20. The close relationship among the polioviruses and CAV11, CAV13, CAV17, CAV20, CAV21, and CAV24 and the uniqueness of CAV1, CAV19, and CAV22 suggest that revisions should be made to the classification of these viruses.

scholarly journals Isolation and characterization of Drosophila multidrug resistance gene homologs.

1991 ◽  
Vol 11 (8) ◽  
pp. 3940-3948 ◽  
Author(s):  
C T Wu ◽  
M Budding ◽  
M S Griffin ◽  
J M Croop
Keyword(s):  
Amino Acid ◽  
Cell Lines ◽  
Multidrug Resistant ◽  
Amino Acid Identity ◽  
Resistant Cell ◽  
Cross Resistance ◽  
Multidrug Resistance Gene ◽  
Isolation And Characterization ◽  
P Glycoprotein

Mammalian multidrug-resistant cell lines, selected for resistance to a single cytotoxic agent, display cross-resistance to a broad spectrum of structurally and functionally unrelated compounds. These cell lines overproduce a membrane protein, the P-glycoprotein, which is encoded by a member(s) of a multigene family, termed mdr or pgp. The amino acid sequence of the P-glycoprotein predicts an energy-dependent transport protein with homology to a large superfamily of proteins which transport a wide variety of substances. This report describes the isolation and characterization of two Drosophila homologs of the mammalian mdr gene. These homologs, located in chromosomal sections 49EF and 65A, encode proteins that share over 40% amino acid identity to the human and murine mdr P-glycoproteins. Fly strains bearing disruptions in the homolog in section 49EF have been constructed and implicate this gene in conferring colchicine resistance to the organism. This work sets the foundation for the molecular and genetic analysis of mdr homologs in Drosophila melanogaster.

scholarly journals Isolation and Characterization of Bovine RVA from Northeast China, 2017–2020

Life ◽  
2021 ◽  
Vol 11 (12) ◽  
pp. 1389
Author(s):  
Xi Cheng ◽  
Wei Wu ◽  
Fei Teng ◽  
Yue Yan ◽  
Guiwei Li ◽  
...  
Keyword(s):  
Genetic Diversity ◽  
Amino Acid ◽  
Northeast China ◽  
Epidemiological Data ◽  
Amino Acid Identity ◽  
Amino Acid Sequences ◽  
Acid Identity ◽  
Bovine Rotavirus ◽  
Isolation And Characterization ◽  
Epidemiological Characteristics

Group A rotaviruses (RVAs) are major enteric pathogens causing infections in calves. To investigate the epidemiological characteristics and genetic diversity of bovine rotavirus (BRV), 233 fecal samples were collected from calves with diarrhea in northeast China. The samples were analyzed for sequences encoding the inner capsid protein VP6 (subgroup) and the outer capsid proteins VP7 and VP4 (G and P type, respectively) using RT-PCR. Ten of the 233 samples (4.3%) were identified as BRV positive and were used for virus isolation and sequence analysis, revealing that all strains analyzed were of the G6P[1] genotype. The isolates exhibited high VP6 sequence identity to the USA cow RVA NCDV strain (>99% amino acid identity) and were further shown to be closely related to Japanese cow RVA BRV101 and Israelian human RVA G6P[1] strains, with >99% amino acid identity to VP7 and VP4 proteins, respectively. Comparative analyses of genome-predicted amino acid sequences between the isolates and the NCDV strains indicated that the antigenicity and infectivity of the strains isolated had changed. In this study, BRV genotypes and the genetic diversity among vaccinated cattle herds were monitored to provide epidemiological data and references for early diagnosis, allowing for early detection of new, potentially pathogenic RVA strains.

scholarly journals Isolation and Characterization of a Hantavirus from Lemmus sibiricus: Evidence for Host Switch during Hantavirus Evolution

1999 ◽  
Vol 73 (7) ◽  
pp. 5586-5592 ◽  
Author(s):  
Olli Vapalahti ◽  
Åke Lundkvist ◽  
Vadim Fedorov ◽  
Christopher J. Conroy ◽  
Sirpa Hirvonen ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Level ◽  
Amino Acid Identity ◽  
Rodent Host ◽  
Host Switch ◽  
Acid Identity ◽  
Noncoding Regions ◽  
Isolation And Characterization ◽  
Focus Reduction

ABSTRACT A novel hantavirus, first detected in Siberian lemmings (Lemmus sibiricus) collected near the Topografov River in the Taymyr Peninsula, Siberia (A. Plyusnin et al., Lancet 347:1835–1836, 1996), was isolated in Vero E6 cells and in laboratory-bred Norwegian lemmings (Lemmus lemmus). The virus, named Topografov virus (TOP), was most closely related to Khabarovsk virus (KBR) and Puumala viruses (PUU). In a cross focus reduction neutralization test, anti-TOP Lemmus antisera showed titers at least fourfold higher with TOP than with other hantaviruses; however, a rabbit anti-KBR antiserum neutralized TOP and KBR at the same titer. The TOP M segment showed 77% nucleotide and 88% amino acid identity with KBR and 76% nucleotide and 82% amino acid identity with PUU. However, the homology between TOP and the KBR S segment was disproportionately higher: 88% at the nucleotide level and 96% at the amino acid level. The 3′ noncoding regions of KBR and the TOP S and M segments were alignable except for 113- and 58-nucleotide deletions in KBR. The phylogenetic relationships of TOP, KBR, and PUU and their respective rodent carriers suggest that an exceptional host switch took place during the evolution of these viruses; while TOP and KBR are monophyletic, the respective rodent host species are only distantly related.

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