Analysis of phosphorylation sites of protein kinases in Cryptosporidium

Cryptosporidiosis is a disease caused by apicomplexan parasite genus Cryptosporidium. In humans, disease manifestation ranges from mild to life threatening condition. Protein kinases are a promising drug target for cryptosporidiosis. Protein kinases act on serine, threonine or tyrosine residues of p...

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Main Authors: Barudin, Mohd Aiman, Md Isa, Muhammad Lokman, Mat Yusof, Afzan
Format: Conference or Workshop Item
Language:English
Published: Malaysian Society of Applied Biology, Universiti Kebangsaan Malaysia 2018
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Online Access:http://irep.iium.edu.my/67089/
http://irep.iium.edu.my/67089/
http://irep.iium.edu.my/67089/
http://irep.iium.edu.my/67089/1/67089_Analysis%20of%20phosphorylation%20sites.pdf
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spelling iium-670892018-10-30T02:57:52Z http://irep.iium.edu.my/67089/ Analysis of phosphorylation sites of protein kinases in Cryptosporidium Barudin, Mohd Aiman Md Isa, Muhammad Lokman Mat Yusof, Afzan Q Science (General) Cryptosporidiosis is a disease caused by apicomplexan parasite genus Cryptosporidium. In humans, disease manifestation ranges from mild to life threatening condition. Protein kinases are a promising drug target for cryptosporidiosis. Protein kinases act on serine, threonine or tyrosine residues of proteins leading to phosphorylation. In this study, protein sequences of kinases of Cryptosporidium associated with cryptosporidiosis were retrieved and searched from NCBI GenBank database. The phosphorylation potential of protein kinases in this parasite has been evaluated using NetPhos 3.1 Server software. This software is an artificial neural network method that predicts phosphorylation sites in independent sequences with sensitivity and fidelity in the range from 69% to 96%. Phosphorylation potential of amino acid residues of kinases in Cryptosporidium was studied. The results indicate that specific residues of amino acids in kinases have a phosphorylation potential suggesting that these residues are important target sites in protein kinases based anti-cryptosporidial therapy. The study reveals that serine, threonine and tyrosine residues of protein kinases having phosphorylation potential close to 1 could be an important target for anti-Cryptosporidium therapies. Hence, different species of Cryptosporidium can provide important insights into development of anti-Cryptosporidium drug regime using kinase inhibitors. Malaysian Society of Applied Biology, Universiti Kebangsaan Malaysia 2018-06-29 Conference or Workshop Item PeerReviewed application/pdf en http://irep.iium.edu.my/67089/1/67089_Analysis%20of%20phosphorylation%20sites.pdf Barudin, Mohd Aiman and Md Isa, Muhammad Lokman and Mat Yusof, Afzan (2018) Analysis of phosphorylation sites of protein kinases in Cryptosporidium. In: The 15th Symposium of Malaysian Society of Applied Biology 2018- Translating Applied Biology for Future Sustainability, 29th June- 1st July 2018, Melaka. http://msabsimposium.blogspot.com/p/technical-session.html Article ID 2018007
repository_type Digital Repository
institution_category Local University
institution International Islamic University Malaysia
building IIUM Repository
collection Online Access
language English
topic Q Science (General)
spellingShingle Q Science (General)
Barudin, Mohd Aiman
Md Isa, Muhammad Lokman
Mat Yusof, Afzan
Analysis of phosphorylation sites of protein kinases in Cryptosporidium
description Cryptosporidiosis is a disease caused by apicomplexan parasite genus Cryptosporidium. In humans, disease manifestation ranges from mild to life threatening condition. Protein kinases are a promising drug target for cryptosporidiosis. Protein kinases act on serine, threonine or tyrosine residues of proteins leading to phosphorylation. In this study, protein sequences of kinases of Cryptosporidium associated with cryptosporidiosis were retrieved and searched from NCBI GenBank database. The phosphorylation potential of protein kinases in this parasite has been evaluated using NetPhos 3.1 Server software. This software is an artificial neural network method that predicts phosphorylation sites in independent sequences with sensitivity and fidelity in the range from 69% to 96%. Phosphorylation potential of amino acid residues of kinases in Cryptosporidium was studied. The results indicate that specific residues of amino acids in kinases have a phosphorylation potential suggesting that these residues are important target sites in protein kinases based anti-cryptosporidial therapy. The study reveals that serine, threonine and tyrosine residues of protein kinases having phosphorylation potential close to 1 could be an important target for anti-Cryptosporidium therapies. Hence, different species of Cryptosporidium can provide important insights into development of anti-Cryptosporidium drug regime using kinase inhibitors.
format Conference or Workshop Item
author Barudin, Mohd Aiman
Md Isa, Muhammad Lokman
Mat Yusof, Afzan
author_facet Barudin, Mohd Aiman
Md Isa, Muhammad Lokman
Mat Yusof, Afzan
author_sort Barudin, Mohd Aiman
title Analysis of phosphorylation sites of protein kinases in Cryptosporidium
title_short Analysis of phosphorylation sites of protein kinases in Cryptosporidium
title_full Analysis of phosphorylation sites of protein kinases in Cryptosporidium
title_fullStr Analysis of phosphorylation sites of protein kinases in Cryptosporidium
title_full_unstemmed Analysis of phosphorylation sites of protein kinases in Cryptosporidium
title_sort analysis of phosphorylation sites of protein kinases in cryptosporidium
publisher Malaysian Society of Applied Biology, Universiti Kebangsaan Malaysia
publishDate 2018
url http://irep.iium.edu.my/67089/
http://irep.iium.edu.my/67089/
http://irep.iium.edu.my/67089/
http://irep.iium.edu.my/67089/1/67089_Analysis%20of%20phosphorylation%20sites.pdf
first_indexed 2023-09-18T21:35:15Z
last_indexed 2023-09-18T21:35:15Z
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