2 edition of Proteolytic maturation of vaccinia virus structural proteins found in the catalog.
Proteolytic maturation of vaccinia virus structural proteins
Judy K. VanSlyke
Written in English
|Statement||by Judy K. VanSlyke.|
|The Physical Object|
|Pagination||110 leaves, bound :|
|Number of Pages||110|
The proteolytic maturation of viruses by PCs generally involves the processing of proteins localized on the surface of viral particles, either of non-enveloped or enveloped viruses .The cleavage of the surface viral proteins mostly occurs inside the host cells during virus morphogenesis and before egress, although cleavage by the target-cell PCs can occur extracellularly or during cell entry Cited by: 2. Proteolytic processing of Gag and Pol proteins is incomplete and delayed. Another novel feature is that the catalytic center of the active dimers of cat FV PR consists of D-S/T-Q instead of D-S/T-G, an unprecedented feature of this by:
Vaccinia virus (VACV or VV) is a large, complex, enveloped virus belonging to the poxvirus family. It has a linear, double-stranded DNA genome approximately kbp in length, which encodes approximately dimensions of the virion are roughly × × nm, with a mass of approximately 5–10 fg.. Smallpox was the first disease to be widely prevented by vaccination, due to Class: incertae sedis. Like the major vaccinia virus (VV) core protein precursors, p4b and p25K, the 25 kDa VV A12L late gene product (p17K) is proteolytically maturated at the conserved Ala-Gly-Ala motif. However, the association of the precursor and its cleavage product with the core of mature virion suggests that both of the A12L proteins may be required for virus by: 6.
Vaccinia virus (VACV) has achieved unprecedented success as a live viral vaccine for smallpox which mitigated eradication of the disease. Vaccinia virus has a complex virion morphology and recent advances have been made to answer some of the key outstanding questions, in particular, the origin and biogenesis of the virion membrane, the transformation from immature virion (IV) to mature virus Cited by: A vaccine is a biological preparation that provides active acquired immunity to a particular infectious disease.A vaccine typically contains an agent that resembles a disease-causing microorganism and is often made from weakened or killed forms of the microbe, its toxins, or one of its surface : D
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Title: Proteolytic Maturation of Vaccinia Virus Structural Proteins: Enzyme and Substrate Analysis. Abstract Approved: Dr. Dennis E. Hruby Several vaccinia virus (VV) structural proteins are synthesized as large precursor proteins, subsequently processed.
From these results the following conclusions can be made. Identification of a putative cleavage consensus site suggests that proteolytic processing is an endoproteolytic event. The observation that precursor structural proteins were found within immature particles indicates that the proteinase responsible for cleavage is also : Judy K.
VanSlyke. Proteolytic maturation of vaccinia virus core proteins: identification of a conserved motif at the N termini of the 4b and 25K virion proteins. VanSlyke JK(1), Franke CA, Hruby DE. Author information: (1)Department of Microbiology, Oregon State University, Corvallis Cited by: Proteolytic maturation of vaccinia virus structural proteins This last modification is especially important with regard to the structural proteins of the virus in that they undergo prysis for an infectious virus particle to be formed, a common theme in viral systems.
The fact that assembly has to occur before proteolytic processing of Author: Judy K. VanSlyke. Graduate Thesis Or Dissertation Proteolytic maturation of Vaccinia virus structural proteins: enzyme and substrate analysis Public Deposited AnalyticsAuthor: Stephen S.
Whitehead. Abstract. Proteolytic processing of vaccinia virus core proteins is an essential step in the formation of mature virions and occurs during the process of virion morphogenesis.
In order to investigate how the vaccinia virus (VV) structural proteins become integrated into virus particles during normal maturation, immunological reagents were generated Cited by: Katz E, Moss B (b) Vaccinia virus structural polypeptide derived from a high-molecular-weight precursor: formation and integration into virus particles.
J Virol 6: – PubMed Google Scholar Kleiman JH, Moss B (a) Purification of a protein kinase and two phosphate acceptor proteins from vaccinia by: VanSlyke JK, Franke CA, Hruby DE.
Proteolytic maturation of vaccinia virus core proteins: identification of a conserved motif at the N termini of the 4b and 25K virion proteins. J Gen Virol. Feb; 72 (Pt 2)– Vanslyke JK, Hruby DE.
Immunolocalization of vaccinia virus structural proteins during virion formation. by: Vaccinia virus (VV) undergoes a proteolytic processing to evolve from immature virus particles into intracellular mature virus particles. Most of structural core protein precursors such as p4a.
One of the major obligatory proteolytic pathways that occurs during the vaccinia virus replicative cycle is maturation of the major core protein precursors. Most of the known core protein cleavage events catalyzed by VV proteinase(s) take place relatively close to the N-terminus of the substrate, releasing small peptides that are predicted to be of markedly higher acidity than the liberated mature : Chelsea M.
Byrd, Tové C. Bolken, Dennis E. Hruby. The most abundant vaccinia virus (VV) core protein found within the virion is protein 4a, which represents approximately 14% of the particle's dry weight. The 4a protein is synthesized as a kDa precursor, which is proteolytically processed to a kDa product concomitant with virion by: Graduate Thesis Or Dissertation Proteolytic maturation of vaccinia virus virion-associated proteins: analysis of substrate determinants Public Deposited AnalyticsAuthor: Peiyu Lee.
The formation of a lipoprotein membrane within specialized areas of the cytoplasm is the first visible step in poxvirus morphogenesis.
The A17L viral protein, an essential nonglycosylated membrane component, was predicted to have four centrally located α-helical membrane-spanning by: VanSlyke JK, Franke CA, Hruby DE: Proteolytic maturation of vaccinia virus core proteins: identification of a conserved motif at the N-termini of the 4b and 25 K virion proteins.
J Gen VirolPubMed CrossRef Google ScholarCited by: 4. (c) Papain-treated virus. Bar indicates nm length. ICHIHASHI, TSURUHARA, AND OIE FIG. Structural proteins of vaccinia virus treated with various proteolytic enzymes.
Samples ( Mg each) ofunlabeled vaccinia virus strain IHD-J were treated with proteolytic enzymes (37 60 min). Treatments and titers were: by: In addition, immunoprecipitation analysis of purified virus particles showed that mature products p35 and p15 are major structural proteins.
According to these results, polyprotein processing represents an essential strategy for the maturation of ASFV structural by: Purchase Handbook of Proteolytic Enzymes, Volume 1 - 2nd Edition.
Print Book & E-Book. ISBNBook Edition: 2. Proteolytic maturation of vaccinia virus core proteins: identification of a conserved motif at the N termini of the 4b and 25K virion proteins.
Gen. Virol. Cited by: We have investigated the molecular-level structure of the Vaccinia virion in situ by protein-protein chemical crosslinking, identifying unique-mass crosslink ions at an effective FDR of %.
Vaccinia virus maturation into infectious particles appears to be dependent on the proteolytic processing of at least five viral proteins, each containing a conserved AG*X cleavage motif and each.
Three structural proteins (4a, 4b and 25K) located within the virion core of vaccinia virus are cleavage products of precursor polypeptides (P4a, P4b and P25K) synthesized late in viral infection.The p21 membrane protein of vaccinia virus (VV), encoded by the A17L gene, has been reported to localize on the inner of the two membranes of the intracellular mature virus (IMV).The three major vaccinia virus (VV) virion proteins (4a, 4b, and 25K) are proteolytically matured from larger precursors (P4a, P4b, and P25K) during virus assembly.
Within the precursors, Ala-Gly-X motifs have been noted at the putative processing sites, with cleavage apparently taking place between the Cited by: