scholarly journals THE STABILITY OF VARIOLA VIRUS PROPAGATED IN EMBRYONATED EGGS

1943 ◽  
Vol 78 (4) ◽  
pp. 231-239 ◽  
Author(s):  
John B. Nelson
Keyword(s):  
Vaccinia Virus ◽  
Significant Alteration ◽  
Variola Virus ◽  
Species Identity ◽  
Apparent Change ◽  
The Stability

After 24 transfers in embryonated eggs a strain of variola virus (Chinese) was established in the testis of the rabbit and maintained for 11 passages at intervals of 7 days. Residence in the rabbit testis was not accompanied by any significant alteration in the species identity of the virus. A second strain of variola virus (Minnesota) was transferred 180 times in embryonated eggs with no apparent change in its behavior. Subsequent attempts, however, to maintain this strain in the rabbit by serial testicular passage were unsuccessful. These observations are discussed in relation to the so called transformation of variola to vaccinia virus by animal passage.

scholarly journals Immunological Memory after Exposure to Variola Virus, Monkeypox Virus, and Vaccinia Virus

2007 ◽  
Vol 195 (8) ◽  
pp. 1151-1159 ◽  
Author(s):  
Sumathi Sivapalasingam ◽  
Jeffrey S. Kennedy ◽  
William Borkowsky ◽  
Fred Valentine ◽  
Ming‐Xia Zhan ◽  
...  
Keyword(s):  
Vaccinia Virus ◽  
Immunological Memory ◽  
Variola Virus ◽  
Monkeypox Virus

scholarly journals Characterization of Chimpanzee/Human Monoclonal Antibodies to Vaccinia Virus A33 Glycoprotein and Its Variola Virus Homolog In Vitro and in a Vaccinia Virus Mouse Protection Model

2007 ◽  
Vol 81 (17) ◽  
pp. 8989-8995 ◽  
Author(s):  
Zhaochun Chen ◽  
Patricia Earl ◽  
Jeffrey Americo ◽  
Inger Damon ◽  
Scott K. Smith ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Vaccinia Virus ◽  
Protective Efficacy ◽  
Variola Virus ◽  
Binding Affinities ◽  
Amino Acid Residues ◽  
C Terminus ◽  
20 Nm

ABSTRACT Three distinct chimpanzee Fabs against the A33 envelope glycoprotein of vaccinia virus were isolated and converted into complete monoclonal antibodies (MAbs) with human γ1 heavy-chain constant regions. The three MAbs (6C, 12C, and 12F) displayed high binding affinities to A33 (Kd of 0.14 nM to 20 nM) and may recognize the same epitope, which was determined to be conformational and located within amino acid residues 99 to 185 at the C terminus of A33. One or more of the MAbs were shown to reduce the spread of vaccinia virus as well as variola virus (the causative agent of smallpox) in vitro and to more effectively protect mice when administered before or 2 days after intranasal challenge with virulent vaccinia virus than a previously isolated mouse anti-A33 MAb (1G10) or vaccinia virus immunoglobulin. The protective efficacy afforded by anti-A33 MAb was comparable to that of a previously isolated chimpanzee/human anti-B5 MAb. The combination of anti-A33 MAb and anti-B5 MAb did not synergize the protective efficacy. These chimpanzee/human anti-A33 MAbs may be useful in the prevention and treatment of vaccinia virus-induced complications of vaccination against smallpox and may also be effective in the immunoprophylaxis and immunotherapy of smallpox and other orthopoxvirus diseases.

scholarly journals Ancient Gene Capture and Recent Gene Loss Shape the Evolution of Orthopoxvirus-Host Interaction Genes

mBio ◽  
2021 ◽  
Author(s):  
Tatiana G. Senkevich ◽  
Natalya Yutin ◽  
Yuri I. Wolf ◽  
Eugene V. Koonin ◽  
Bernard Moss
Keyword(s):  
Immune Response ◽  
Vaccinia Virus ◽  
Gene Loss ◽  
Genome Replication ◽  
Variola Virus ◽  
Human Pathogens ◽  
Gene Capture ◽  
Host Interaction ◽  
Virion Morphogenesis ◽  
Ancient Gene

Orthopoxviruses (ORPV) include smallpox (variola) virus, one of the most devastating human pathogens, and vaccinia virus, comprising the vaccine used for smallpox eradication. Among roughly 200 ORPV genes, about half are essential for genome replication and expression as well as virion morphogenesis, whereas the remaining half consists of accessory genes counteracting the host immune response.

scholarly journals Effect of NaCl on the Stability of Oncolytic Vaccinia Virus

2016 ◽  
Vol 26 (1) ◽  
pp. 23-33 ◽  
Author(s):  
Seong-Geun Kim ◽  
Gui Shao Ran ◽  
Hyuk-Chan Kwon ◽  
Tae-Ho Hwang
Keyword(s):  
Vaccinia Virus ◽  
The Stability

scholarly journals Variola virus F1L is a Bcl-2-like protein that unlike its vaccinia virus counterpart inhibits apoptosis independent of Bim

2015 ◽  
Vol 6 (3) ◽  
pp. e1680-e1680 ◽  
Author(s):  
B Marshall ◽  
H Puthalakath ◽  
S Caria ◽  
S Chugh ◽  
M Doerflinger ◽  
...  
Keyword(s):  
Vaccinia Virus ◽  
Variola Virus

scholarly journals Genetic and Cell Biological Characterization of the Vaccinia Virus A30 and G7 Phosphoproteins

2005 ◽  
Vol 79 (11) ◽  
pp. 7146-7161 ◽  
Author(s):  
Jason Mercer ◽  
Paula Traktman
Keyword(s):  
Vaccinia Virus ◽  
Temperature Sensitive ◽  
Phenotypic Analysis ◽  
Virion Morphogenesis ◽  
Release Assay ◽  
The Stability ◽  
Temperature Sensitive Phenotype

ABSTRACT The vaccinia virus proteins A30 and G7 are known to play essential roles in early morphogenesis, acting prior to the formation of immature virions. Their repression or inactivation results in the accumulation of large virosomes, detached membrane crescents, and empty immature virions. We have undertaken further study of these proteins to place them within the context of the F10 kinase, the A14 membrane protein, and the H5 phosphoprotein, which have been the focus of previous studies within our laboratory. Here we confirm that both A30 and G7 undergo F10 kinase-dependent phosphorylation in vivo and recapitulate that modification of A30 in vitro. Although the detached crescents observed upon loss of A30 or G7 echo those seen upon repression of A14, no interaction between A30/G7 and A14 could be detected. We did, however, determine that the A30 and G7 proteins are unstable during nonpermissive tsH5 infections, suggesting that the loss of A30/G7 is the underlying cause for the formation of lacy or curdled virosomes. We also determined that the temperature-sensitive phenotype of the Cts11 virus is due to mutations in two codons of the G7L gene. Phenotypic analysis of nonpermissive Cts11 infections indicated that these amino acid substitutions compromise G7 function without impairing the stability of either G7 or A30. Utilizing Cts11 in conjunction with a rifampin release assay, we determined that G7 acts at multiple stages of virion morphogenesis that can be distinguished both by ultrastructural analysis and by monitoring the phosphorylation status of several viral proteins that undergo F10-mediated phosphorylation.

scholarly journals Species Specificity of Vaccinia Virus Complement Control Protein for the Bovine Classical Pathway Is Governed Primarily by Direct Interaction of Its Acidic Residues with Factor I

2017 ◽  
Vol 91 (19) ◽  
Author(s):  
Jitendra Kumar ◽  
Viveka Nand Yadav ◽  
Swastik Phulera ◽  
Ashish Kamble ◽  
Avneesh Kumar Gautam ◽  
...  
Keyword(s):  
Vaccinia Virus ◽  
Classical Pathway ◽  
Variola Virus ◽  
Complement Control Protein ◽  
Factor I ◽  
Functional Assays ◽  
Alternative Complement ◽  
Cofactor Activity ◽  
Complement Regulator ◽  
Control Protein

ABSTRACTPoxviruses display species tropism—variola virus is a human-specific virus, while vaccinia virus causes repeated outbreaks in dairy cattle. Consistent with this, variola virus complement regulator SPICE (smallpox inhibitor of complement enzymes) exhibits selectivity in inhibiting the human alternative complement pathway and vaccinia virus complement regulator VCP (vaccinia virus complement control protein) displays selectivity in inhibiting the bovine alternative complement pathway. In the present study, we examined the species specificity of VCP and SPICE for the classical pathway (CP). We observed that VCP is ∼43-fold superior to SPICE in inhibiting bovine CP. Further, functional assays revealed that increased inhibitory activity of VCP for bovine CP is solely due to its enhanced cofactor activity, with no effect on decay of bovine CP C3-convertase. To probe the structural basis of this specificity, we utilized single- and multi-amino-acid substitution mutants wherein 1 or more of the 11 variant VCP residues were substituted in the SPICE template. Examination of these mutants for their ability to inhibit bovine CP revealed that E108, E120, and E144 are primarily responsible for imparting the specificity and contribute to the enhanced cofactor activity of VCP. Binding and functional assays suggested that these residues interact with bovine factor I but not with bovine C4(H2O) (a moiety conformationally similar to C4b). Mapping of these residues onto the modeled structure of bovine C4b-VCP-bovine factor I supported the mutagenesis data. Taken together, our data help explain why the vaccine strain of vaccinia virus was able to gain a foothold in domesticated animals.IMPORTANCEVaccinia virus was used for smallpox vaccination. The vaccine-derived virus is now circulating and causing outbreaks in dairy cattle in India and Brazil. However, the reason for this tropism is unknown. It is well recognized that the virus is susceptible to neutralization by the complement classical pathway (CP). Because the virus encodes a soluble complement regulator, VCP, we examined whether this protein displays selectivity in targeting bovine CP. Our data show that it does exhibit selectivity in inhibiting the bovine CP and that this is primarily determined by its amino acids E108, E120, and E144, which interact with bovine serine protease factor I to inactivate bovine C4b—one of the two subunits of CP C3-convertase. Of note, the variola complement regulator SPICE contains positively charged residues at these positions. Thus, these variant residues in VCP help enhance its potency against the bovine CP and thereby the fitness of the virus in cattle.

scholarly journals The stability of the serotypes ofBordetella pertussiswith particular reference to serotype 1,2,3,4

1976 ◽  
Vol 76 (2) ◽  
pp. 277-286 ◽  
Author(s):  
Caroline J. Bronne–Shanbury ◽  
Jean M. Dolby
Keyword(s):  
Bordetella Pertussis ◽  
Heterogeneous Group ◽  
Mixed Cultures ◽  
Apparent Change ◽  
The Stability ◽  
Stable Variable

SUMMARYStrains ofBordetella pertussisin which all the organisms contain agglutinogens 1 and 3 or 1, 2 and 4 are easy to identify as serotypes 1,0,3,0 and 1,2,0,4 respectively; and similarly, stable strains of serotype 1,0,3,4 are occasionally found. During repeated subcultures, passagein vivo, and lyophilization and preservation for many years, these serotypes do not change. Mixing 1,0,3,0 and 1,2,0,4 serotypes and culturing them togetherin vivoandin vitroproduces cultures from which organisms of the same two serotypes can be isolated.In contrast, strains which type as 1,2,3,4 are often a heterogeneous group. We have attempted to classify these as 'stable', 'variable' and 'mixed' cultures. Some strains comprise organisms all of which contain the four agglutinogens and are as easy to type as the strains described above. These we have called 'stable' 1,2,3,4 strains. Other 1,2,3,4 strains are made up of colonies possessing all four agglutinogens, as shown by agglutinin production, but in amounts varying from day to day so that direct typing is inconsistent. These we have called 'variable' 1,2,3,4 strains. The last category, 'mixed', is made up of organisms most of which give rise to stable 1,2,3,4 cultures; a few of the component organisms, however, have one or two of the four agglutinogens missing. The importance of the 'variable' cultures is emphasized for work on apparent change of serotype, e.g. during infection.

scholarly journals Low-Resolution Structure of Vaccinia Virus DNA Replication Machinery

2012 ◽  
Vol 87 (3) ◽  
pp. 1679-1689 ◽  
Author(s):  
Céleste Sèle ◽  
Frank Gabel ◽  
Irina Gutsche ◽  
Ivan Ivanov ◽  
Wim P. Burmeister ◽  
...  
Keyword(s):  
Vaccinia Virus ◽  
Recombinant Expression ◽  
Rotational Symmetry ◽  
Vaccination Campaign ◽  
Virus Genome ◽  
Genome Replication ◽  
Variola Virus ◽  
Replication Machinery ◽  
Content Type ◽  
Rolling Circle

ABSTRACTSmallpox caused by the poxvirus variola virus is a highly lethal disease that marked human history and was eradicated in 1979 thanks to a worldwide mass vaccination campaign. This virus remains a significant threat for public health due to its potential use as a bioterrorism agent and requires further development of antiviral drugs. The viral genome replication machinery appears to be an ideal target, although very little is known about its structure. Vaccinia virus is the prototypic virus of theOrthopoxvirusgenus and shares more than 97% amino acid sequence identity with variola virus. Here we studied four essential viral proteins of the replication machinery: the DNA polymerase E9, the processivity factor A20, the uracil-DNA glycosylase D4, and the helicase-primase D5. We present the recombinant expression and biochemical and biophysical characterizations of these proteins and the complexes they form. We show that the A20D4 polymerase cofactor binds to E9 with high affinity, leading to the formation of the A20D4E9 holoenzyme. Small-angle X-ray scattering yielded envelopes for E9, A20D4, and A20D4E9. They showed the elongated shape of the A20D4 cofactor, leading to a 150-Å separation between the polymerase active site of E9 and the DNA-binding site of D4. Electron microscopy showed a 6-fold rotational symmetry of the helicase-primase D5, as observed for other SF3 helicases. These results favor a rolling-circle mechanism of vaccinia virus genome replication similar to the one suggested for tailed bacteriophages.

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