The best-known mechanism of action of antibody-mediated virus neutralization is to impede the entrance of viruses to host cells, as determined by neutralization assays. Antibodies may also inhibit the exit of rubella virus (RV) from infected host cells; in this case, the interaction of the antibodies with their domains must occur on the plasma membrane, because antibodies cannot enter the cells. In the present study, we were able to block temporally the exit of virions from RV-infected cells by the binding of monoclonal antibody (mAb) H3 to their surface. The objective was accomplished in three steps: first, we determined the duration of the viral replication cycle; then we established the kinetics of the presence of the domains defined by our mAbs in the cytoplasm of RV-infected VERO cells; and, finally, we assessed the release of viral particles to the supernatant of infected VERO cells in the presence or absence of mAbs or positive and negative mice sera. RV-specific mice sera and mAb H3, which binds to the amino acid sequence 208-239 of the RV-E1 glycoprotein, were able to delay for 24 hours the release of virions from infected cultures, suggesting that the reaction of mAb H3 with its epitope may arrest any change necessary for the assembly and/or release of virions. In conclusion, the neutralizing domain recognized by mAb induces antibodies that can block the viral replication by several mechanisms of action, such as the obstruction of virus entry into cells and the delay of viral release. All of these mechanisms are intimately involved in the critical virus-host cell interactions that allow self-limitation of the infection.
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http://dx.doi.org/10.1089/vim.2000.13.83 | DOI Listing |
Mikrobiyol Bul
January 2025
Kocaeli Üniversitesi Tıp Fakültesi, Tıbbi Mikrobiyoloji Anabilim Dalı, Kocaeli.
Son yıllarda pandemi nedeniyle virüslerin tanı ve tedavisine yönelik terapötik yöntemlerin geliştirilmesi ve antivirallerin test edilmesi amacıyla çok sayıda in vitro çalışma yapılmaktadır. Literatürde SARS-CoV-2'nin modellenebilmesi için HCoV-229E'nin kullanımının güvenli ve yeterli olup olmadığını inceleyen çalışmalar sınırlıdır. Bu sebeple bu çalışmada, BSL-2 şartlarında gerçekleştirilebilen HCoV-229E kültürü ve kantitasyon çalışmalarının, BSL-3 şartları gerektiren SARS-CoV-2 deneylerinde bir ön çalışma modeli olup olamayacağının antiviral etkinlik analizleri üzerinden araştırılması amaçlanmıştır.
View Article and Find Full Text PDFTrop Biomed
December 2024
Department of Medical Microbiology, Faculty of Medicine, Universiti Malaya, 50603 Kuala Lumpur, Malaysia.
Dengue, caused by the dengue virus (DENV), poses a significant global health challenge. Effective vaccines and treatments for dengue are lacking due to gaps in understanding its pathogenesis and mechanisms in severe cases. This study investigates the role of immunoglobulin E (IgE) in dengue, focusing on its potential association with virus neutralization and antibody-dependent enhancement (ADE) in DENV replication.
View Article and Find Full Text PDFACS Omega
January 2025
Department of Industrial Chemistry, Faculty of Applied Science, King Mongkut's University of Technology North Bangkok, Bangkok 10800, Thailand.
Our phytochemical investigation of the roots of led to the isolation of two new lanostane triterpenes, 3-acetylpolycarpol () and 15-acetylpolycarpol (), as well as 15 known compounds (-). The structures of the isolated compounds were elucidated by an analysis of spectroscopic data. Compounds - were tested against nonsmall cell lung cancer cells (A549) and human cervical carcinoma cells (HeLa) using an MTT assay.
View Article and Find Full Text PDFMicrob Pathog
January 2025
Department of Laboratory Medicine, Suzhou Mental Health Center, the Affiliated Guangji Hospital of Soochow University, Suzhou215137, Jiangsu, China.
Enterovirus 71 (EV-71) is a major pathogenic factor that causes hand, foot, and mouth disease in young children and infants. Given the limited treatments for EV-71 infection, discovering new host factors and understanding the mechanisms involved will aid in combating this viral infection. Neutral sphingomyelinase-2 (nSMase-2, encoded by SMPD3) is a crucial cellular cofactor in viral infection.
View Article and Find Full Text PDFSci Rep
January 2025
Department of Pathology, Division of Microbiology, Faculty of Veterinary Medicine, Wroclaw University of Environmental and Life Sciences, 50-375, Wroclaw, Poland.
The process of viral entry into host cells is crucial for the establishment of infection and the determination of viral pathogenicity. A comprehensive understanding of entry pathways is fundamental for the development of novel therapeutic strategies. Standard techniques for investigating viral entry include confocal microscopy and flow cytometry, both of which provide complementary qualitative and quantitative data.
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