IFITMs of African Green Monkey Can Inhibit Replication of SFTSV but Not MNV In Vitro

2020 ◽  
Vol 33 (10) ◽  
pp. 634-641
Author(s):  
Huanwei Xing ◽  
Li Ye ◽  
Junwen Fan ◽  
Tingting Fu ◽  
Chang Li ◽  
...  
Keyword(s):  
African Green Monkey ◽  
Green Monkey

Characterization of Cadmium-Induced Metallothionein in African Green Monkey Kidney Cells In Vitro

1979 ◽  
pp. 187-196 ◽  
Author(s):  
Masami Kimura ◽  
Noriko Otaki ◽  
Tsuyoshi Kakefuda
Keyword(s):  
African Green Monkey ◽  
Monkey Kidney ◽  
Kidney Cells ◽  
African Green Monkey Kidney ◽  
Green Monkey

scholarly journals Identification and Characterization of an Adeno-Associated Virus Integration Site in CV-1 Cells from the African Green Monkey

2003 ◽  
Vol 77 (3) ◽  
pp. 1904-1915 ◽  
Author(s):  
Terry J. Amiss ◽  
Doug M. McCarty ◽  
Anna Skulimowski ◽  
R. Jude Samulski
Keyword(s):  
Integration Site ◽  
Binding Activity ◽  
African Green Monkey ◽  
Pcr Analysis ◽  
Adeno Associated Virus ◽  
Biochemical Basis ◽  
Green Monkey ◽  
Latently Infected

ABSTRACT Adeno-associated virus (AAV) is a classification given to a group of nonpathogenic, single-stranded DNA viruses known to reside latently in primates. During latency in humans, AAV type 2 (AAV2) preferentially integrates at a site on chromosome 19q13.3ter by targeting a sequence composed of an AAV Rep binding element (RBE), a spacer, and a nicking site. Here, we report the DNA sequence of an African green monkey AAV integration site isolated from CV-1 cells. Overall, it has 98% homology to the analogous human site, including identical spacer and nicking sequences. However, the simian RBE is expanded, having five perfect directly repeated GAGC tetramers. We carried out a number of in vitro and in vivo assays to determine the effect of this expanded RBE sequence on the Rep-RBE interaction and AAV targeted integration. Using electromobility shift assays it was demonstrated that AAV4 Rep68 bound the expanded RBE with a sixfold-greater affinity than the human RBE. To determine the basis for the affinity increase, DNase I protection and methylation interference (MI) assays were performed. Comparison of footprints on both the human and simian RBEs revealed nearly identical protection; however, MI analysis suggested greater interaction with the guanine nucleotides of the expanded RBE, thus providing a biochemical basis for the increased binding activity. In vivo, integration targeted to the simian RBE was demonstrated by PCR analysis of latently infected Cos-7 cells. Interestingly, the frequency of site-specific integration was twofold greater in Cos-7 cells than in HeLa cells. Overall, these experiments establish that the simian RBE, identified in CV-1 cells, functions analogously to the human RBE and provide further evidence for a developing model that proposes individual roles for the RBE and the spacer and nicking site elements.

Genotoxic and cytotoxic effects of the drug dipyrone sodium in African green monkey kidney (Vero) cell line exposed in vitro

2021 ◽  
Author(s):  
Lorena M. Gomes ◽  
Daniele A. Moysés ◽  
Henrique F. S. Nascimento ◽  
Tatiane C. Mota ◽  
Lais T. Bonfim ◽  
...  
Keyword(s):  
Vero Cell ◽  
Cell Line ◽  
African Green Monkey ◽  
Monkey Kidney ◽  
Cytotoxic Effects ◽  
African Green Monkey Kidney ◽  
Vero Cell Line ◽  
Green Monkey

scholarly journals Genetic Identity and Biological Phenotype of a Transmitted/Founder Virus Representative of Nonpathogenic Simian Immunodeficiency Virus Infection in African Green Monkeys

2010 ◽  
Vol 84 (23) ◽  
pp. 12245-12254 ◽  
Author(s):  
Clement Wesley Gnanadurai ◽  
Ivona Pandrea ◽  
Nicholas F. Parrish ◽  
Matthias H. Kraus ◽  
Gerald H. Learn ◽  
...  
Keyword(s):  
Simian Immunodeficiency Virus ◽  
Consensus Sequence ◽  
African Green Monkey ◽  
Productive Infection ◽  
Peripheral Blood Mononuclear ◽  
Immunodeficiency Virus ◽  
Green Monkey ◽  
Viral Determinants

ABSTRACT Understanding the lack of disease progression in nonpathogenic simian immunodeficiency virus (SIV) infections is essential for deciphering the immunopathogenesis of human AIDS. Yet, in vivo studies have been hampered by a paucity of infectious molecular clones (IMCs) of SIV suitable to dissect the viral and host factors responsible for the nonpathogenic phenotype. Here, we describe the identification, cloning, and biological analysis of the first transmitted/founder (T/F) virus representing a nonpathogenic SIV infection. Blood was collected at peak viremia from an acutely infected sabaeus monkey (Chlorocebus sabaeus) inoculated intravenously with an African green monkey SIV (SIVagm) strain (Sab92018) that had never been propagated in vitro. To generate IMCs, we first used conventional (bulk) PCR to amplify full-length viral genomes from peripheral blood mononuclear cell (PBMC) DNA. Although this yielded two intact SIVagmSab genomes, biological characterization revealed that both were replication defective. We then performed single-genome amplification (SGA) to generate partially overlapping 5′ (n = 10) and 3′ (n = 13) half genomes from plasma viral RNA. Analysis of these amplicons revealed clusters of nearly identical viral sequences representing the progeny of T/F viruses. Synthesis of the consensus sequence of one of these generated an IMC (Sab92018ivTF) that produced infectious CCR5-tropic virions and replicated to high titers in Molt-4 clone 8 cells and African green monkey PBMCs. Sab92018ivTF also initiated productive infection in sabaeus monkeys and faithfully recapitulated the replication kinetics and nonpathogenic phenotype of the parental Sab92018 strain. These results thus extend the T/F virus concept to nonpathogenic SIV infections and provide an important new tool to define viral determinants of disease nonprogression.

Characterization of an EBV-like virus from African green monkey lymphoblasts

Virology ◽  
1980 ◽  
Vol 101 (1) ◽  
pp. 291-295 ◽  
Author(s):  
J.F. Bocker ◽  
K.-H. Tiedemann ◽  
G.W. Bornkamm ◽  
H. Zur Hausen
Keyword(s):  
African Green Monkey ◽  
Green Monkey

CYP2B6 is expressed in African Green monkey brain and is induced by chronic nicotine treatment

2006 ◽  
Vol 50 (4) ◽  
pp. 441-450 ◽  
Author(s):  
Anna M. Lee ◽  
Sharon Miksys ◽  
Roberta Palmour ◽  
Rachel F. Tyndale
Keyword(s):  
African Green Monkey ◽  
Nicotine Treatment ◽  
Monkey Brain ◽  
Chronic Nicotine ◽  
Green Monkey ◽  
Chronic Nicotine Treatment

Characterization of angiotensin II binding sites in African Green monkey uterus

Life Sciences ◽  
1985 ◽  
Vol 36 (2) ◽  
pp. 177-182 ◽  
Author(s):  
Ernest P. Petersen ◽  
John W. Wright ◽  
Joseph W. Harding
Keyword(s):  
Angiotensin Ii ◽  
Binding Sites ◽  
African Green Monkey ◽  
Green Monkey

Surface expression of influenza virus neuraminidase, an amino-terminally anchored viral membrane glycoprotein, in polarized epithelial cells

1985 ◽  
Vol 5 (9) ◽  
pp. 2181-2189
Author(s):  
L V Jones ◽  
R W Compans ◽  
A R Davis ◽  
T J Bos ◽  
D P Nayak
Keyword(s):  
Influenza Virus ◽  
Influenza A ◽  
Surface Expression ◽  
African Green Monkey ◽  
Monkey Kidney ◽  
Kidney Cells ◽  
African Green Monkey Kidney ◽  
Amino Terminal ◽  
Green Monkey ◽  
Na Gene

We have investigated the site of surface expression of the neuraminidase (NA) glycoprotein of influenza A virus, which, in contrast to the hemagglutinin, is bound to membranes by hydrophobic residues near the NH2-terminus. Madin-Darby canine kidney or primary African green monkey kidney cells infected with influenza A/WSN/33 virus and subsequently labeled with monoclonal antibody to the NA and then with a colloidal gold- or ferritin-conjugated second antibody exhibited specific labeling of apical surfaces. Using simian virus 40 late expression vectors, we also studied the surface expression of the complete NA gene (SNC) and a truncated NA gene (SN10) in either primary or a polarized continuous line (MA104) of African green monkey kidney cells. The polypeptides encoded by the cloned NA cDNAs were expressed on the surface of both cell types. Analysis of [3H]mannose-labeled polypeptides from recombinant virus-infected MA104 cells showed that the products of cloned NA cDNA comigrated with glycosylated NA from influenza virus-infected cells. Both the complete and the truncated glycoproteins were found to be preferentially expressed on apical plasma membranes, as detected by immunogold labeling. These results indicate that the NA polypeptide contains structural features capable of directing the transport of the protein to apical cell surfaces and the first 10 amino-terminal residues of the NA polypeptide are not involved in this process.

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