Specifications
Species Reactivity
Adenovirus
Immunogen
Purified Adenovirus hexon. The Adenovirus type is not known.
Applications
General Notes
Adenovirus hexon is the major capsid protein that forms the outer shell of the virus, playing a crucial role in viral assembly, stability, and immune recognition. This monoclonal antibody recognizes the hexon group antigen across 34 Adenovirus serotypes, including types 40 and 41.
Images
Cells were infected with Ad5 virus and subjected to IF staining using Adenovirus antibody (Cat.No DMABT-Z59148) at serial dilutions. Cells were fixed with 4% PFA, permeabilized with Triton X-100, and blocked with 1% BSA. Antibody incubation was performed at room temperature for 1 hour in the dark. Nuclei were counterstained with DAPI (blue), and antibody signal was visualized via FITC (green).
Target
Alternative Names
Adenovirus; Adenoviridae; Aviadenovirus; ADENOVIRUS; ADENOVIRUS F
Citations
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Adenoviruses (AdV) are DNA viruses that typically cause mild infections involving the upper or lower respiratory tract, gastrointestinal (GI) tract, or conjunctiva. Rare manifestations of AdV infections include hemorrhagic cystitis, hepatitis, hemorrhagic colitis, pancreatitis, nephritis, or encephalitis. Adenovirus infections are more common in young children, owing to lack of humoral immunity. Epidemics of AdV infections may occur in healthy children or adults in closed or crowded settings. The disease is more severe, and dissemination is more likely in patients with impaired immunity (eg, organ transplant recipients, human immunodeficiency virus infection, congenital immunodeficiency syndromes). Fatality rates for untreated severe AdV pneumonia or disseminated disease may exceed 50%. More than 50 serotypes of AdV have been identified. Different serotypes display different tissue trophisms and correlate with clinical manifestations of infection.
Figure 1. Structure of adenovirus hexon.
(Source: Susan L. Pichla-Gollon. et al., 2007.)
The adenovirus capsid consists of three major structural proteins: hexon, penton, and fiber. A total of 240 hexon capsomeres forms the majority of the capsid structure, whereas 12 vertex capsomeres consist of the fiber attachment proteins and their penton bases. Hexon-specific Abs have been shown by several laboratories to exert significant neutralizing activity in vitro. Adenovirus-neutralizing antibodies can be raised against any of the major capsid proteins. However, experiments with chimeric viruses-in which capsid components of one serotype were replaced by those of another serotype-suggest that hexon is the predominant target of serotype-specific neutralizing antibodies.
References
1. Susan L. Pichla-Gollon. et al., Structure-Based Identification of a Major Neutralizing Site in an Adenovirus Hexon. J Virol. 2007 Feb;81(4):1680-1689.
2. Shawn M. Sumida. et al., Neutralizing Antibodies to Adenovirus Serotype 5 Vaccine Vectors Are Directed Primarily against the Adenovirus Hexon Protein. J Immunol. 2005 June, 174 (11): 7179–7185.
Dynamic competition for hexon binding between core protein VII and lytic protein VI promotes adenovirus maturation and entry
PNAS
Authors: Mercedes Hernando-Pérez, Natalia Martín-González, Marta Pérez-Illana, Maarit Suomalainen.
Abstract
Adenovirus minor coat protein VI contains a membrane-disruptingpeptide that is inactive when VI is bound to hexon trimers. ProteinVI must be released during entry to ensure endosome escape. Hex-on:VI stoichiometry has been uncertain, and only fragments of VIhave been identified in the virion structure. Recent findings suggestan unexpected relationship between VI and the major core protein,VII. According to the high-resolution structure of the mature virion,VI and VII may compete for the same binding site in hexon; andnoninfectious human adenovirus type 5 particles assembled in theabsence of VII (Ad5-VII-) are deficient in proteolytic maturation ofprotein VI and endosome escape. Here we show that Ad5-VII- par-ticles are trapped in the endosome because they fail to increase VIexposure during entry. This failure was not due to increased particlestability, because capsid disruption happened at lower thermal ormechanical stress in Ad5-VII- compared to wild-type (Ad5-wt) parti-cles. Cryoelectron microscopy difference maps indicated that VII canoccupy the same binding pocket as VI in all hexon monomers,strongly arguing for binding competition. In the Ad5-VII- map, den-sity corresponding to the immature amino-terminal region of VIindicates that in the absence of VII the lytic peptide is trapped insidethe hexon cavity, and clarifies the hexon:VI stoichiometry conun-drum. We propose a model where dynamic competition betweenproteins VI and VII for hexon binding facilitates the complete mat-uration of VI, and is responsible for releasing the lytic protein fromthe hexon cavity during entry and stepwise uncoating.
Identification of potent epitopes on hexon capsid protein and their evaluation as vaccine candidates against infections caused by members of Adenoviridae family,Vaccine
Vaccine
Authors: Soban Tufail, Majid Ali Shah, Maryam Zafar, Tayyab Ali Asif, Aamir Shehzad, Muhammad Salahuddin Shah, Mudasser Habib, Muhammad Kashif Saleemi, Muhammad Muddassar, Osman Mirza, Mazhar Iqbal, Moazur Rahman
Abstract
Adenoviruses cause economically important diseases in vertebrates. Effective vaccines against adenoviral diseases are currently lacking. Here, we report a highly conserved epitopic region on hexon proteins of adenoviruses that generate a strong immune response when used as a virus-like-particle (VLP) vaccine, produced by inserting the epitopic region into the core protein of hepatitis B virus. For evaluation of its protective efficacy, the epitopic region from a representative adenovirus, fowl adenovirus serotype 4 (FAdV-4), was tested as a VLP vaccine which conferred 90% protection against challenge with a virulent FAdV-4 isolate in chickens. Importantly, such a high level of protection is not achieved when the epitopic region is employed as a part of a subunit vaccine. As the sequence and the structure of the epitopic region are highly conserved in hexon proteins of adenoviruses, the epitopic region could be employed as a promising VLP vaccine candidate against adenoviral diseases, in general.
Reagents for Adenovirus Assay Development 
Certificate of Analysis
