Nucleotide variations of Streptococcus pneumoniae hyaluronate lyase (spnhyl) gene in clinical isolates

Ahmad Yusof @ Hanafi, Hanani and Masri, Siti Norbaya and Mohd Desa, Mohd Nasir and Osman, Malina and Jamal, Farida (2012) Nucleotide variations of Streptococcus pneumoniae hyaluronate lyase (spnhyl) gene in clinical isolates. In: 31st Symposium of the Malaysian Society for Microbiology, 13th-15th Dec. 2012, Promenade Hotel, Kota Kinabalu, Sabah. (Unpublished)

	PDF - Accepted Version Restricted to Repository staff only Download (108kB) | Request a copy
	PDF (p.11) - Supplemental Material Restricted to Repository staff only Download (1MB) | Request a copy
	PDF - Presentation Restricted to Repository staff only Download (1MB) | Request a copy

Abstract

Streptococcus pneumoniae is an important cause of human infections, particularly pneumonia, acute otitis media and meningitis. Hyaluronate lyase, an enzyme secreted by Streptococcus pneumoniae facilitates bacterial invasion by degradation of host connective tissue. This study was conducted to characterize the nucleotide sequence of hyaluronate lyase gene among clinical isolates of Streptococcus pneumoniae. Twenty isolates were selected comprising 13 from blood, 3 from sputum, 2 from pus and one each from cerebrospinal fluid and pleural fluid. ATCC 49169 strain was included as the positive control. DNA was extracted from all samples and PCR amplification was done using 5 sets of primers prior to sequencing the whole gene. DNA sequence analysis was done with BioEdit, NCBI Blast tools and MEGA4 software by using Streptococcus pneumoniae TIGR4 as the reference sequence. A total of 100 nucleotide variants were found among the strains which comprised 98 single nucleotide substitutions, 1 deletion and 1 insertion of triplet bases. From this result it was predicted that 53 variants could change the amino acid residue. Part of the changes involved 15 residues of both α- and β-domains, and 1 residue in the linker. Two nucleotide variations could cause earlier stop codon. Although high numbers of nucleotide variants were present, biological function of hyaluronate lyase was not likely to be affected as no catalytic active site was involved. The nucleotide variants were scattered in all strains, and did not appear to be related to the serotype or clinical source of the strain. Further studies are required to elaborate the significance of these findings.

Item Type:	Conference or Workshop Item (Speech/Talk)
Additional Information:	7232/45442
Uncontrolled Keywords:	Streptococcus pneumoniae Hyaluronate Lyase (spnhyl)
Subjects:	Q Science > QR Microbiology
Kulliyyahs/Centres/Divisions/Institutes (Can select more than one option. Press CONTROL button):	Kulliyyah of Allied Health Sciences > Department of Biomedical Science (Effective:1st July 2011)
Depositing User:	Dr Hanani Ahmad Yusof @ Hanafi
Date Deposited:	23 Nov 2015 15:48
Last Modified:	28 Jun 2016 14:17
URI:	http://irep.iium.edu.my/id/eprint/45442

Actions (login required)

View Item