Highly soluble and stable ‘insertion domain’ of the capsid penton base protein provides complete protection against infections caused by fowl adenoviruses

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Highly soluble and stable ‘insertion domain’ of the capsid penton base protein provides complete protection against infections caused by fowl adenoviruses. / 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.

In: Microbial Pathogenesis, Vol. 173, No. Part A, 105835, 2022.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Tufail, S, Shah, MA, Asif, TA, Ullah, R, Shehzad, A, Ismat, F, Shah, MS, Habib, M, Calisto, BM, Mirza, O, Iqbal, M & Rahman, M 2022, 'Highly soluble and stable ‘insertion domain’ of the capsid penton base protein provides complete protection against infections caused by fowl adenoviruses', Microbial Pathogenesis, vol. 173, no. Part A, 105835. https://doi.org/10.1016/j.micpath.2022.105835

APA

Tufail, S., Shah, M. A., Asif, T. A., Ullah, R., Shehzad, A., Ismat, F., Shah, M. S., Habib, M., Calisto, B. M., Mirza, O., Iqbal, M., & Rahman, M. (2022). Highly soluble and stable ‘insertion domain’ of the capsid penton base protein provides complete protection against infections caused by fowl adenoviruses. Microbial Pathogenesis, 173(Part A), [105835]. https://doi.org/10.1016/j.micpath.2022.105835

Vancouver

Tufail S, Shah MA, Asif TA, Ullah R, Shehzad A, Ismat F et al. Highly soluble and stable ‘insertion domain’ of the capsid penton base protein provides complete protection against infections caused by fowl adenoviruses. Microbial Pathogenesis. 2022;173(Part A). 105835. https://doi.org/10.1016/j.micpath.2022.105835

Author

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. / Highly soluble and stable ‘insertion domain’ of the capsid penton base protein provides complete protection against infections caused by fowl adenoviruses. In: Microbial Pathogenesis. 2022 ; Vol. 173, No. Part A.

Bibtex

@article{68182fbd52bc4e3d9005bbec33b3ee76,
title = "Highly soluble and stable {\textquoteleft}insertion domain{\textquoteright} of the capsid penton base protein provides complete protection against infections caused by fowl adenoviruses",
abstract = "In the current study, we have evaluated the protective efficacy of the {\textquoteleft}insertion domain{\textquoteright} which is commonly found in the capsid penton base protein of many adenoviruses. Using the {\textquoteleft}insertion domain{\textquoteright} of the penton base protein of a representative fowl adenovirus, fowl adenovirus serotype 4 (FAdV-4), we find that the {\textquoteleft}insertion domain{\textquoteright} 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 {\textquoteleft}insertion domain{\textquoteright}, 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{\texttrademark} 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 {\textquoteleft}insertion domain{\textquoteright} 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.",
author = "Soban Tufail and Shah, {Majid Ali} and Asif, {Tayyab Ali} and Raheem Ullah and Aamir Shehzad and Fouzia Ismat and Shah, {Muhammad Salahuddin} and Mudasser Habib and Calisto, {B{\'a}rbara M.} and Osman Mirza and Mazhar Iqbal and Moazur Rahman",
year = "2022",
doi = "10.1016/j.micpath.2022.105835",
language = "English",
volume = "173",
journal = "Microbial Pathogenesis",
issn = "0882-4010",
publisher = "Academic Press",
number = "Part A",

}

RIS

TY - JOUR

T1 - Highly soluble and stable ‘insertion domain’ of the capsid penton base protein provides complete protection against infections caused by fowl adenoviruses

AU - Tufail, Soban

AU - Shah, Majid Ali

AU - Asif, Tayyab Ali

AU - Ullah, Raheem

AU - Shehzad, Aamir

AU - Ismat, Fouzia

AU - Shah, Muhammad Salahuddin

AU - Habib, Mudasser

AU - Calisto, Bárbara M.

AU - Mirza, Osman

AU - Iqbal, Mazhar

AU - Rahman, Moazur

PY - 2022

Y1 - 2022

N2 - 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.

AB - 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.

U2 - 10.1016/j.micpath.2022.105835

DO - 10.1016/j.micpath.2022.105835

M3 - Journal article

C2 - 36265735

VL - 173

JO - Microbial Pathogenesis

JF - Microbial Pathogenesis

SN - 0882-4010

IS - Part A

M1 - 105835

ER -

ID: 322952582