Mutation of domain III and domain VI in L gene conserved domain of Nipah virus

Siti Aishah Jalani, Nazlina Ibrahim

Research output: Chapter in Book/Report/Conference proceedingConference contribution

Abstract

Nipah virus (NiV) is the etiologic agent responsible for the respiratory illness and causes fatal encephalitis in human. NiV L protein subunit is thought to be responsible for the majority of enzymatic activities involved in viral transcription and replication. The L protein which is the viral RNA dependent RNA polymerase has high sequence homology among negative sense RNA viruses. In negative stranded RNA viruses, based on sequence alignment six conserved domain (domain I-IV) have been determined. Each domain is separated on variable regions that suggest the structure to consist concatenated functional domain. To directly address the roles of domains III and VI, site-directed mutations were constructed by the substitution of bases at sequences 2497, 2500, 5528 and 5532. Each mutated L gene can be used in future studies to test the ability for expression on in vitro translation.

Original languageEnglish
Title of host publication2016 UKM FST Postgraduate Colloquium: Proceedings of the Universiti Kebangsaan Malaysia, Faculty of Science and Technology 2016 Postgraduate Colloquium
PublisherAmerican Institute of Physics Inc.
Volume1784
ISBN (Electronic)9780735414464
DOIs
Publication statusPublished - 17 Nov 2016
Event2016 Postgraduate Colloquium of the Universiti Kebangsaan Malaysia, Faculty of Science and Technology, UKM FST 2016 - Selangor, Malaysia
Duration: 13 Apr 201614 Apr 2016

Other

Other2016 Postgraduate Colloquium of the Universiti Kebangsaan Malaysia, Faculty of Science and Technology, UKM FST 2016
CountryMalaysia
CitySelangor
Period13/4/1614/4/16

Fingerprint

viruses
mutations
genes
encephalitis
proteins
homology
alignment
substitutes
causes

ASJC Scopus subject areas

  • Physics and Astronomy(all)

Cite this

Jalani, S. A., & Ibrahim, N. (2016). Mutation of domain III and domain VI in L gene conserved domain of Nipah virus. In 2016 UKM FST Postgraduate Colloquium: Proceedings of the Universiti Kebangsaan Malaysia, Faculty of Science and Technology 2016 Postgraduate Colloquium (Vol. 1784). [020018] American Institute of Physics Inc.. https://doi.org/10.1063/1.4966728

Mutation of domain III and domain VI in L gene conserved domain of Nipah virus. / Jalani, Siti Aishah; Ibrahim, Nazlina.

2016 UKM FST Postgraduate Colloquium: Proceedings of the Universiti Kebangsaan Malaysia, Faculty of Science and Technology 2016 Postgraduate Colloquium. Vol. 1784 American Institute of Physics Inc., 2016. 020018.

Research output: Chapter in Book/Report/Conference proceedingConference contribution

Jalani, SA & Ibrahim, N 2016, Mutation of domain III and domain VI in L gene conserved domain of Nipah virus. in 2016 UKM FST Postgraduate Colloquium: Proceedings of the Universiti Kebangsaan Malaysia, Faculty of Science and Technology 2016 Postgraduate Colloquium. vol. 1784, 020018, American Institute of Physics Inc., 2016 Postgraduate Colloquium of the Universiti Kebangsaan Malaysia, Faculty of Science and Technology, UKM FST 2016, Selangor, Malaysia, 13/4/16. https://doi.org/10.1063/1.4966728
Jalani SA, Ibrahim N. Mutation of domain III and domain VI in L gene conserved domain of Nipah virus. In 2016 UKM FST Postgraduate Colloquium: Proceedings of the Universiti Kebangsaan Malaysia, Faculty of Science and Technology 2016 Postgraduate Colloquium. Vol. 1784. American Institute of Physics Inc. 2016. 020018 https://doi.org/10.1063/1.4966728
Jalani, Siti Aishah ; Ibrahim, Nazlina. / Mutation of domain III and domain VI in L gene conserved domain of Nipah virus. 2016 UKM FST Postgraduate Colloquium: Proceedings of the Universiti Kebangsaan Malaysia, Faculty of Science and Technology 2016 Postgraduate Colloquium. Vol. 1784 American Institute of Physics Inc., 2016.
@inproceedings{121d8ca6e36448059b78167bc8998f3f,
title = "Mutation of domain III and domain VI in L gene conserved domain of Nipah virus",
abstract = "Nipah virus (NiV) is the etiologic agent responsible for the respiratory illness and causes fatal encephalitis in human. NiV L protein subunit is thought to be responsible for the majority of enzymatic activities involved in viral transcription and replication. The L protein which is the viral RNA dependent RNA polymerase has high sequence homology among negative sense RNA viruses. In negative stranded RNA viruses, based on sequence alignment six conserved domain (domain I-IV) have been determined. Each domain is separated on variable regions that suggest the structure to consist concatenated functional domain. To directly address the roles of domains III and VI, site-directed mutations were constructed by the substitution of bases at sequences 2497, 2500, 5528 and 5532. Each mutated L gene can be used in future studies to test the ability for expression on in vitro translation.",
author = "Jalani, {Siti Aishah} and Nazlina Ibrahim",
year = "2016",
month = "11",
day = "17",
doi = "10.1063/1.4966728",
language = "English",
volume = "1784",
booktitle = "2016 UKM FST Postgraduate Colloquium: Proceedings of the Universiti Kebangsaan Malaysia, Faculty of Science and Technology 2016 Postgraduate Colloquium",
publisher = "American Institute of Physics Inc.",

}

TY - GEN

T1 - Mutation of domain III and domain VI in L gene conserved domain of Nipah virus

AU - Jalani, Siti Aishah

AU - Ibrahim, Nazlina

PY - 2016/11/17

Y1 - 2016/11/17

N2 - Nipah virus (NiV) is the etiologic agent responsible for the respiratory illness and causes fatal encephalitis in human. NiV L protein subunit is thought to be responsible for the majority of enzymatic activities involved in viral transcription and replication. The L protein which is the viral RNA dependent RNA polymerase has high sequence homology among negative sense RNA viruses. In negative stranded RNA viruses, based on sequence alignment six conserved domain (domain I-IV) have been determined. Each domain is separated on variable regions that suggest the structure to consist concatenated functional domain. To directly address the roles of domains III and VI, site-directed mutations were constructed by the substitution of bases at sequences 2497, 2500, 5528 and 5532. Each mutated L gene can be used in future studies to test the ability for expression on in vitro translation.

AB - Nipah virus (NiV) is the etiologic agent responsible for the respiratory illness and causes fatal encephalitis in human. NiV L protein subunit is thought to be responsible for the majority of enzymatic activities involved in viral transcription and replication. The L protein which is the viral RNA dependent RNA polymerase has high sequence homology among negative sense RNA viruses. In negative stranded RNA viruses, based on sequence alignment six conserved domain (domain I-IV) have been determined. Each domain is separated on variable regions that suggest the structure to consist concatenated functional domain. To directly address the roles of domains III and VI, site-directed mutations were constructed by the substitution of bases at sequences 2497, 2500, 5528 and 5532. Each mutated L gene can be used in future studies to test the ability for expression on in vitro translation.

UR - http://www.scopus.com/inward/record.url?scp=85014693054&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85014693054&partnerID=8YFLogxK

U2 - 10.1063/1.4966728

DO - 10.1063/1.4966728

M3 - Conference contribution

AN - SCOPUS:85014693054

VL - 1784

BT - 2016 UKM FST Postgraduate Colloquium: Proceedings of the Universiti Kebangsaan Malaysia, Faculty of Science and Technology 2016 Postgraduate Colloquium

PB - American Institute of Physics Inc.

ER -