scholarly journals Peptidic Inhibitors for in Vitro Pentamer Formation of Human Papillomavirus Capsid Protein L1

2015 ◽  
Vol 6 (4) ◽  
pp. 381-385 ◽  
Author(s):  
Ding-Yi Fu ◽  
Shi Jin ◽  
Dong-Dong Zheng ◽  
Xiao Zha ◽  
Yuqing Wu
Keyword(s):  
Human Papillomavirus ◽  
Capsid Protein ◽  
Peptidic Inhibitors

scholarly journals Human Papillomavirus E2 Regulates SRSF3 (SRp20) To Promote Capsid Protein Expression in Infected Differentiated Keratinocytes

2016 ◽  
Vol 90 (10) ◽  
pp. 5047-5058 ◽  
Author(s):  
T. Klymenko ◽  
H. Hernandez-Lopez ◽  
A. I. MacDonald ◽  
J. M. Bodily ◽  
S. V. Graham
Keyword(s):  
Human Papillomavirus ◽  
Life Cycle ◽  
Protein Expression ◽  
Capsid Protein ◽  
Drug Targets ◽  
Cell Metabolism ◽  
Dependent Manner ◽  
Control Activity

ABSTRACTThe human papillomavirus (HPV) life cycle is tightly linked to differentiation of the infected epithelial cell, suggesting a sophisticated interplay between host cell metabolism and virus replication. Previously, we demonstrated in differentiated keratinocytesin vitroandin vivothat HPV type 16 (HPV16) infection caused increased levels of the cellular SR splicing factors (SRSFs) SRSF1 (ASF/SF2), SRSF2 (SC35), and SRSF3 (SRp20). Moreover, the viral E2 transcription and replication factor that is expressed at high levels in differentiating keratinocytes could bind and control activity of the SRSF1 gene promoter. Here, we show that the E2 proteins of HPV16 and HPV31 control the expression of SRSFs 1, 2, and 3 in a differentiation-dependent manner. E2 has the greatest transactivation effect on expression of SRSF3. Small interfering RNA depletion experiments in two different models of the HPV16 life cycle (W12E and NIKS16) and one model of the HPV31 life cycle (CIN612-9E) revealed that only SRSF3 contributed significantly to regulation of late events in the virus life cycle. Increased levels of SRSF3 are required for L1 mRNA and capsid protein expression. Capsid protein expression was regulated specifically by SRSF3 and appeared independent of other SRSFs. Taken together, these data suggest a significant role of the HPV E2 protein in regulating late events in the HPV life cycle through transcriptional regulation of SRSF3 expression.IMPORTANCEHuman papillomavirus replication is accomplished in concert with differentiation of the infected epithelium. Virus capsid protein expression is confined to the upper epithelial layers so as to avoid immune detection. In this study, we demonstrate that the viral E2 transcription factor activates the promoter of the cellular SRSF3 RNA processing factor. SRSF3 is required for expression of the E4^L1 mRNA and so controls expression of the HPV L1 capsid protein. Thus, we reveal a new dimension of virus-host interaction crucial for production of infectious virus. SRSF proteins are known drug targets. Therefore, this study provides an excellent basis for developing strategies to regulate capsid protein production in the infected epithelium and the production of new virions.

scholarly journals Mounting evidence of the efficacy of human papillomavirus vaccines

2006 ◽  
Vol 11 (19) ◽  
Author(s):  
Collective Editorial team
Keyword(s):  
Human Papillomavirus ◽  
Capsid Protein ◽  
Self Assembly ◽  
Vaccine Candidate ◽  
Papillomavirus Vaccines ◽  
Human Papillomavirus Vaccines ◽  
Virus Like Particles

Since virus-like particles (VLP) generated by the synthesis and self-assembly in vitro of the major human papillomavirus (HPV) capsid protein (L1) were shown to work in principle as a vaccine candidate

Refolding and in vitro characterization of human papillomavirus 16 minor capsid protein L2

2019 ◽  
Vol 400 (4) ◽  
pp. 513-522 ◽  
Author(s):  
Bastian Breiner ◽  
Laura Preuss ◽  
Nora Roos ◽  
Marcel Conrady ◽  
Hauke Lilie ◽  
...  
Keyword(s):  
Human Papillomavirus ◽  
Capsid Protein ◽  
Viral Entry ◽  
Analytical Ultracentrifugation ◽  
Transmembrane Region ◽  
Hpv 16 ◽  
High Tendency ◽  
Minor Capsid Protein

Abstract The minor capsid protein L2 of papillomaviruses exhibits multiple functions during viral entry including membrane interaction. Information on the protein is scarce, because of its high tendency of aggregation. We determined suitable conditions to produce a functional human papillomavirus (HPV) 16 L2 protein and thereby provide the opportunity for extensive in vitro analysis with respect to structural and biochemical information on L2 proteins and mechanistic details in viral entry. We produced the L2 protein of high-risk HPV 16 in Escherichia coli as inclusion bodies and purified the protein under denaturing conditions. A successive buffer screen resulted in suitable conditions for the biophysical characterization of 16L2. Analytical ultracentrifugation of the refolded protein showed a homogenous monomeric species. Furthermore, refolded 16L2 shows secondary structure elements. The N-terminal region including the proposed transmembrane region of 16L2 shows alpha-helical characteristics. However, overall 16L2 appears largely unstructured. Refolded 16L2 is capable of binding to DNA indicating that the putative DNA-binding regions are accessible in refolded 16L2. Further the refolded protein interacts with liposomal membranes presumably via the proposed transmembrane region at neutral pH without structural changes. This indicates that 16L2 can initially interact with membranes via pre-existing structural features.

A fluorescence-enhanced inorganic probe to detect the peptide and capsid protein of human papillomavirus in vitro

RSC Advances ◽  
2016 ◽  
Vol 6 (34) ◽  
pp. 28612-28618 ◽  
Author(s):  
Teng Zhang ◽  
Ding-Yi Fu ◽  
Yuqing Wu ◽  
Yizhan Wang ◽  
Lixin Wu
Keyword(s):  
Human Papillomavirus ◽  
Capsid Protein ◽  
L1 Protein

A europium-substituted polyoxometalate (EuW10) could be used as a fluorescence-enhanced probe to detect the recombinant HPV L1 protein in vitro.

IN VITRO SENSITIZATION TO HUMAN PAPILLOMAVIRUS TYPE 18 PEPTIDES

1999 ◽  
Vol 22 (5) ◽  
pp. 456
Author(s):  
M. R. Castellanos ◽  
M. A. Maiman ◽  
R. L. Hayes
Keyword(s):  
Human Papillomavirus

scholarly journals Specific Recognition of a Stem-Loop RNA Structure by the Alphavirus Capsid Protein

Viruses ◽  
2021 ◽  
Vol 13 (8) ◽  
pp. 1517
Author(s):  
Rebecca S. Brown ◽  
Lisa Kim ◽  
Margaret Kielian
Keyword(s):  
Capsid Protein ◽  
Rna Structure ◽  
Semliki Forest Virus ◽  
Virus Assembly ◽  
Specific Binding ◽  
Genomic Rna ◽  
Stem Loop ◽  
Stem Loop Structure ◽  
Labeled Rna

Alphaviruses are small enveloped viruses with positive-sense RNA genomes. During infection, the alphavirus capsid protein (Cp) selectively packages and assembles with the viral genomic RNA to form the nucleocapsid core, a process critical to the production of infectious virus. Prior studies of the alphavirus Semliki Forest virus (SFV) showed that packaging and assembly are promoted by Cp binding to multiple high affinity sites on the genomic RNA. Here, we developed an in vitro Cp binding assay based on fluorescently labeled RNA oligos. We used this assay to explore the RNA sequence and structure requirements for Cp binding to site #1, the top binding site identified on the genomic RNA during all stages of virus assembly. Our results identify a stem-loop structure that promotes specific binding of the SFV Cp to site #1 RNA. This structure is also recognized by the Cps of the related alphaviruses chikungunya virus and Ross River virus.

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