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Human papillomavirus (HPV) is a small, non-enveloped, and circular virus with a double-stranded DNA genome of about 8,000 base pairs that are covered with capsid proteins. HPV primarily infects mucosal and cutaneous epithelia in multiple higher vertebrates in a species-specific manner and induces cellular proliferation. These viruses are known to play a significant role in various cancers, particularly cervical cancer. To comprehend the mechanisms of HPV infection, it is essential to examine the proteins involved in this intricate process, which is crucial for developing effective vaccines, diagnostic tools, and therapeutic interventions.
Figure 1. The structure of human papillomavirus (HPV) and its function.
(Source: Lee, S. J. et al., 2016)
The early (E) proteins of HPV, including E1, E2, E4, E5, E6, and E7, are critical regulators of viral replication. These proteins work in tandem to ensure the successful establishment and maintenance of viral episomes within the host cells.
E1 and E2: viral replication and transcription regulation
The E1 and E2 proteins are key regulators of HPV replication and transcription. The E1 protein acts as a helicase and is responsible for initiating viral DNA replication by unwinding the DNA strands at the origin of replication. It forms a complex with viral DNA and recruits the cellular factors necessary for replication. The E2 protein acts as a transcriptional regulator and plays a vital role in controlling viral gene expression. It binds to specific DNA sequences in the viral genome, known as E2 binding sites, and regulates the transcription of viral genes, including E6 and E7 oncogenes.
E4: viral morphogenesis and cellular cytoskeletal changes
The E4 protein is expressed late in the viral life cycle and is associated with the differentiation of infected epithelial cells. E4 interacts with and disrupts the organization of intermediate filaments, mitochondria, the cornified cell envelope (CCE), and ND10 domains. These proteins have been reported to be involved in the regulation of late gene expression, facilitating and supporting viral genome amplification, the control of virus maturation, and the mediation of virus release.
E5: modulation of cellular signaling and immune evasion
The E5 protein of high-risk HPV types is a small hydrophobic protein that is localized to the endoplasmic reticulum and Golgi apparatus. It is known to modulate various cellular signaling pathways, including the epidermal growth factor receptor (EGFR) pathway. E5 can interact with and activate EGFR, leading to increased cell proliferation and survival, which are important for viral replication. Additionally, E5 has been shown to interfere with the immune response by downregulating the expression of major histocompatibility complex class I (MHC-I) molecules on the surface of infected cells, thereby evading immune recognition.
E6 and E7: oncoproteins with transforming potential
The E6 and E7 oncoproteins are the most extensively studied HPV proteins due to their critical role in HPV-associated oncogenesis. High-risk HPV types, such as HPV 16 and HPV 18, produce E6 and E7 proteins that contribute to the development of cervical and other anogenital cancers. The dysregulation caused by E6 and E7 proteins can result in genomic instability, accumulation of genetic mutations, and ultimately contribute to the development of HPV-associated cancers.
The L (late) proteins of Human Papillomavirus (HPV) are involved in the late stages of the viral life cycle, particularly in the assembly of viral capsids.
L1 Protein: Major Structural Protein of Viral Capsids
The L1 protein is the major capsid protein of HPV and plays a critical role in the assembly of viral capsids. It forms the majority of the capsid structure and is responsible for the icosahedral symmetry of the viral particle. L1 proteins self-assemble to form capsomers, which further assemble into the icosahedral capsid structure that encloses the viral genome. The L1 capsomers are arranged in a lattice structure, providing stability and protection to the viral DNA.
L2 Protein: Capsid Assembly and Genome Packaging
The L2 protein is another important protein involved in the capsid assembly process and genome packaging. Although less abundant than L1, L2 interacts with L1 and assists in the assembly of viral capsids. It is also involved in the encapsidation of viral DNA into the capsid during the generation of progeny virions. L2 has been shown to interact with cellular components, such as dynein and cyclophilins, to facilitate viral trafficking and uncoating within infected cells.
The L1 and L2 proteins are attractive targets for vaccination strategies against HPV infection. Vaccines based on L1 virus-like particles (VLPs) have been developed and proven to be highly effective in preventing HPV infection. L1 VLPs closely resemble the structure of the native viral capsids, but they lack the viral genome, making them non-infectious. When administered as a vaccine, L1 VLPs stimulate a strong immune response, including the production of neutralizing antibodies, which can prevent the entry of HPV into host cells. These vaccines have demonstrated significant efficacy in preventing HPV infection, genital warts, and HPV-associated cancers, such as cervical, vulvar, vaginal, anal, and oropharyngeal cancers.
Learn more about Recombinant HPV L1 VLP
Learn more about HPV L1 Antibodies for Neutralization and Vaccine Development
Understanding the proteins necessary for HPV infection provides insights into viral pathogenesis, informs public health strategies, and plays a crucial role in combating HPV-associated diseases, including cervical and other types of cancer. With our cutting-edge tools and steadfast HPV antibodies, antigens, and ELISA kits, Creative Diagnostics empowers researchers and healthcare professionals to make significant strides in combating HPV-related diseases.
References
| Target | Cat. No. | Product Name | Expression System | Tag/Conjugate | Application | |
| HPV | PSVG-HPV16 | Pseudotyped GFP HPV16 | Useful for studying papillomavirus assembly, entry, and neutralization. | Inquiry | ||
| PSVG-HPV18 | Pseudotyped GFP HPV18 | Useful for studying papillomavirus assembly, entry, and neutralization. | Inquiry | |||
| PSVG-HPV31 | Pseudotyped GFP HPV31 | Useful for studying papillomavirus assembly, entry, and neutralization. | Inquiry | |||
| PSVG-HPV33 | Pseudotyped GFP HPV33 | Useful for studying papillomavirus assembly, entry, and neutralization. | Inquiry | |||
| PSVG-HPV39 | Pseudotyped GFP HPV39 | Useful for studying papillomavirus assembly, entry, and neutralization. | Inquiry | |||
| PSVG-HPV45 | Pseudotyped GFP HPV45 | Useful for studying papillomavirus assembly, entry, and neutralization. | Inquiry | |||
| HPV 11 | DAGF-228 | Recombinant Human Papilloma Virus type 11 L1 protein (VLP) | E. coli | Unconjugated | Inquiry | |
| DAG1576 | Recombinant HPV type 11 [GST] | E. coli | GST | N/A | Inquiry | |
| HPV 35 | DAGC142 | Recombinant Human Papilloma Virus type 35 L1 protein (VLP) | E. coli | Unconjugated | SDS-PAGE | Inquiry |
| HPV 39 | DAGC143 | Recombinant Human Papilloma Virus type 39 L1 protein (VLP) | E. coli | Unconjugated | SDS-PAGE | Inquiry |
| HPV16 | DAGF-094 | Recombinant HPV16 E6 protein [His] | E. coli | His | Inquiry | |
| DAGF-095 | Recombinant HPV16 E6 protein (aa 1-158) [His] | Yeast | His | Inquiry | ||
| DAGF-096 | Recombinant HPV16 E7 protein (aa 1-98) [GST] | E. coli | GST | Inquiry | ||
| DAGF-229 | Recombinant Human Papilloma Virus type 16 L1 protein (VLP) | E. coli | Unconjugated | Inquiry | ||
| DAG-P2512 | Recombinant HPV type 16 (aa 1 - 531) | E. coli | Unconjugated | SDS-PAGE | Inquiry |
| Target | Cat. No. | Product Name | Size | Species Reactivity | Application | Detection Sample | |
| HPV | DEIA-F678S | Human Papilloma Virus IgG ELISA kit | 96T | Human | Qualitative | plasma, serum | Inquiry |
| DEIASL404 | Human HPV18 IgM ELISA kit | 96T | Qualitative | Serum, plasma | Inquiry | ||
| DEIASL405 | Human HPV 16 L1-capsids IgG ELISA Kit | 96T | Qualitative | Serum, plasma | Inquiry | ||
| DEIASL406 | Human HPV 16 IgM ELISA Kit | 96T | Qualitative | Serum, plasma | Inquiry | ||
| DEIASL407 | Human Papilloma Virus IgM ELISA Kit | 96T | Qualitative | Serum, plasma | Inquiry | ||
| DEIASL408 | Human HPV 18 L1-capsids IgG ELISA Kit | 96T | Qualitative | Serum, plasma | Inquiry | ||
| DEIASL409 | Rabbit HPV 16 L1-capsids IgG ELISA Kit | 96T | Qualitative | Serum, plasma | Inquiry | ||
| DEIASL410 | Human high risk HPV L1-capsids (HR-HPVL1) IgG ELISA kit | 96T | Qualitative | Serum, plasma | Inquiry | ||
| DEIASL119 | HPV(18) Antigen ELISA Quantitation Kit | 96T | Quantitative | Serum, plasma | Inquiry | ||
| DEIASL120 | HPV(52) Antigen ELISA Quantitation Kit | 96T | Quantitative | Serum, plasma | Inquiry | ||
| DEIASL121 | HPV(58) Antigen ELISA Quantitation Kit | 96T | Quantitative | Serum, plasma | Inquiry | ||
| DEIASL171 | Human HPV 16 E7 Oncoprotein ELISA Kit | 96T | Human | Quantitative | Cell lysates, tissue lysates, cervical smears, plasma, serum | Inquiry | |
| DEIASL172 | Human HPV 18 E7 Oncoprotein ELISA Kit | 96T | Quantitative | Cell lysates, tissue lysates, or cervical smears | Inquiry | ||
| HPV16 | DEIASL118 | HPV (16) Antigen ELISA Quantitation Kit | 96T | Human | Quantitative | Serum and plasma | Inquiry |
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