Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/15937
Title: PE-PGRS proteins in mycobacterial pathogenicity and host response
Authors: KOH KAH WEE
Keywords: tuberculosis, vaccine, host-pathogen interaction, antigen processing, PE-PGRS proteins, cellular immune response
Issue Date: 17-Apr-2009
Source: KOH KAH WEE (2009-04-17). PE-PGRS proteins in mycobacterial pathogenicity and host response. ScholarBank@NUS Repository.
Abstract: The functions of the unique PE-PGRS protein family in mycobacteria are largely unknown. The proteins have a conserved N-terminal Pro-Glu (PE) domain and C-terminal polymorphic GC-rich repetitive sequences (PGRS). We investigated immune responses directed against two such proteins and their roles in host-pathogen interactions. The stability of PE-PGRS proteins against degradation was also studied. Active or latent tuberculosis patients showed strong antibody responses to Rv3812PE-PGRS, but not to Rv0978cPE-PGRS. The PGRS domain protected the highly unstable Rv0978cPE from proteolytic degradation, influencing antigen processing for CD8+ T cell recognition. Rv3812PE-PGRS protein was identified as a surface protein without involvement in mycobacterium cell entry. Cellular immune responses to the PGRS but not the PE domain were observed in mycobacterium-infected mice. Murine immunisation with Rv3812PE-PGRS induced B and T cell responses to both domains. The roles elucidated for PE-PGRS proteins in host-pathogen interactions are relevant to immunodiagnosis and immunoprophylaxis of early tuberculosis infection.
URI: http://scholarbank.nus.edu.sg/handle/10635/15937
Appears in Collections:Ph.D Theses (Open)

Show full item record
Files in This Item:
File Description SizeFormatAccess SettingsVersion 
KohKW.pdf1.9 MBAdobe PDF

OPEN

NoneView/Download

Page view(s)

286
checked on Dec 11, 2017

Download(s)

465
checked on Dec 11, 2017

Google ScholarTM

Check


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.