Background: Viruses included in the family Iridoviridae are large, icosahedral, dsDNA viruses that are subdivided into 5 genera. Frog virus 3 (FV3) is the type species of the genus Ranavirus and the best studied iridovirus at the molecular level. Typically, antibodies directed against a virus act to neutralize the virus and limit infection. Antibody dependent enhancement occurs when viral antibodies enhance infectivity of the virus rather than neutralize it.
Results: Here we show that anti-FV3 serum present at the time of FV3 infection enhances infectivity of the virus in two non-immune teleost cell lines. We found that antibody dependent enhancement of FV3 was dependent on the Fc portion of anti-FV3 antibodies but not related to complement. Furthermore, the presence of anti-FV3 serum during an FV3 infection in a non-immune mammalian cell line resulted in neutralization of the virus. Our results suggest that a cell surface receptor specific to teleost cell lines is responsible for the enhancement.
Conclusions: This report represents the first evidence of antibody dependent enhancement in iridoviruses. The data suggests that anti-FV3 serum can either neutralize or enhance viral infection and that enhancement is related to a novel antibody dependent enhancement pathway found in teleosts that is Fc dependent.
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http://dx.doi.org/10.1186/1743-422X-7-41 | DOI Listing |
Front Immunol
January 2025
Department of Hematology and Transplantology, Medical University of Gdansk, Gdansk, Poland.
Background: Paroxysmal nocturnal hemoglobinuria (PNH) is a rare complement-driven acquired hemolytic anemia with specific presentations of hemoglobinuria, abdominal pain, fatigue, and thrombosis.
Objective: To review the current therapeutic strategies for PNH, including anti-complement therapy and allogeneic hematopoietic cell transplantation (alloHCT), focusing on the tailoring of the approach to the disease subtype.
Results: The outcome of alloHCT varies depending on disease severity, thrombotic history, and response to prior therapies.
Small Methods
January 2025
NEST, Istituto Nanoscienze - CNR and Scuola Normale Superiore, Pisa, I-56127, Italy.
A ground-breaking graphene-based biosensor designed for label-free detection of immunoglobulin M (IgM) achieving a remarkable concentration of 100 zeptomolar (10 m), is reported. The sensor is a two-terminal device and incorporates a millimeter-wide gold interface, bio-functionalized with ≈10 anti-IgM antibodies and capacitively coupled to a bare graphene electrode through a water-soaked paper strip. In this configuration, few affinity binding events trigger a collective electrostatic reorganization of the protein layer, leading to an extended surface potential (SP) shift of the biofunctionalized Au surface.
View Article and Find Full Text PDFJ Chromatogr A
January 2025
Center of Molecular Immunology, 216 Street and 15th Avenue Atabey-Siboney Playa P.O. Box 16040, Havana, 11600, Cuba. Electronic address:
Protein A chromatography represents the most prevalent methodology for the capture of monoclonal antibodies. The use of a low pH elution buffer from Protein A has been observed to contribute to product aggregation, particularly in the case of IgG4 antibodies, such as nivolumab. This paper presents a well-defined strategy for addressing this issue.
View Article and Find Full Text PDFBiomedica
December 2024
Grupo Red de Donación y Trasplantes, Instituto Nacional de Salud, Bogotá, D. C., Colombia.
Introduction. The use of immunological tests before solid organ transplantation is essential to reduce the risk of rejection and post-transplant complications. Therefore, quality control systems in laboratories performing them are necessary for clinical practice.
View Article and Find Full Text PDFPLoS Pathog
January 2025
Institute of Medical Virology, University of Zurich (UZH), Zurich, Switzerland.
For use in prevention and treatment, HIV-1 broadly neutralizing antibodies (bnAbs) have to overcome Env conformational heterogeneity of viral quasispecies and neutralize with constant high potency. Comparative analysis of neutralization data from the CATNAP database revealed a nuanced relationship between bnAb activity and Env conformational flexibility, with substantial epitope-specific variation of bnAb potency ranging from increased to decreased activity against open, neutralization-sensitive Env. To systematically investigate the impact of variability in Env conformation on bnAb potency we screened 126 JR-CSF point mutants for generalized neutralization sensitivity to weakly neutralizing antibodies (weak-nAbs) depending on trimer opening and plasma from people with chronic HIV-1 infection.
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