Highly soluble and stable 'insertion domain' of the capsid penton base protein provides complete protection against infections caused by fowl adenoviruses. (December 2022)

• Record Type: Journal Article
• Authors: Tufail, Soban; Shah, Majid Ali; Asif, Tayyab Ali; Ullah, Raheem; Shehzad, Aamir; Ismat, Fouzia; Shah, Muhammad Salahuddin; Habib, Mudasser; Calisto, Bárbara M.; Mirza, Osman; Iqbal, Mazhar; Rahman, Moazur
• Is Part Of: Microbial pathogenesis. Volume 173(2022)Part A
• Publication Date: 2022-12
• Subjects: Fowl adenovirus -- Penton base -- Subunit vaccine -- Insertion domain -- Hydropericardium syndrome; Pathogenic microorganisms -- Periodicals; Pathology, Molecular -- Periodicals; Communicable Diseases -- microbiology -- Periodicals; Communicable Diseases -- parasitology -- Periodicals; Micro-organismes pathogènes -- Périodiques; Pathologie moléculaire -- Périodiques; Electronic journals; 616.9041
• DOI: 10.1016/j.micpath.2022.105835
• Languages: English
• ISSNs: 0882-4010

Abstract

Abstract: In the current study, we have evaluated the protective efficacy of the 'insertion domain' which is commonly found in the capsid penton base protein of many adenoviruses. Using the 'insertion domain' of the penton base protein of a representative fowl adenovirus, fowl adenovirus serotype 4 (FAdV-4), we find that the 'insertion domain' can readily be expressed in a soluble form in the bacterial system, and can be purified in sufficient quantities through simple chromatographic methods. We demonstrate that the 'insertion domain', when employed as a subunit vaccine candidate, provides complete protection against hydropericardium syndrome, caused by FAdV-4, in chickens. The data presented here indicate that the protein, adjuvanted with Montanide™ ISA71 VG, provides complete protection in chickens against a lethal FAdV-4 challenge after administration of two doses (100 μg of the protein per dose) two weeks apart (the first dose at the 7th day of life and a booster dose at the age of 21 days). Furthermore, the purified protein can be stored at low temperatures without any observable loss in the protein integrity up to one year, tested so far. Due to the conserved nature of the 'insertion domain' across the penton base protein of fowl adenoviruses, it is suggested that homologous insertion domains could be employed as highly stable and cost-effective subunit vaccine candidates against infections caused by respective fowl adenoviruses. Graphical abstract: Image 1 Highlights: Identification of insertion domain in penton base proteins as a protective antigen. Overexpression of highly conserved insertion domain in a soluble form in E. coli . Insertion domain provides complete protection against fowl adenovirus (FAdV-4). The purified domain can be stored at low temperatures up to one year. Insertion domain could be employed as subunit vaccine against fowl adenoviruses.