Sweeten PAMPs: role of sugar complexed PAMPs in innate immunity and vaccine biology
- 1Laboratory of Immunology, Department of Biological Sciences, Indian Institute of Science Education and Research (IISER), Bhopal, India
- 2Department of Biotechnology and Bioinformatics, Yogi Vemana University, Kadapa, India
- 3Department of Microbiology, Yogi Vemana University, Kadapa, India
- 4WPI Immunology Frontier Research Center, Osaka University, Osaka, Japan
Innate sensors play a critical role in the early innate immune responses to invading pathogens through sensing of diverse biochemical signatures also known as pathogen associated molecular patterns (PAMPs). These biochemical signatures primarily consist of a major family of biomolecules such as proteins, lipids, nitrogen bases, and sugar and its complexes, which are distinct from host molecules and exclusively expressed in pathogens and essential to their survival. The family of sensors known as pattern recognition receptors (PRRs) are germ-line encoded, evolutionarily conserved molecules, and consist of Toll-like receptors (TLRs), RIG-I-like receptors (RLRs), NOD-like receptors (NLRs), C-type lectin-like receptors (CLRs), and DNA sensors. Sensing of PAMP by PRR initiates the cascade of signaling leading to the activation of transcription factors, such as NF-κB and interferon regulatory factors (IRFs), resulting in a variety of cellular responses, including the production of interferons (IFNs) and pro-inflammatory cytokines. In this review, we discuss sensing of different types of glycosylated PAMPs such as β-glucan (a polymeric sugar) or lipopolysaccharides, nucleic acid, and so on (sugar complex PAMPs) by different families of sensors, its role in pathogenesis, and its application in development of potential vaccine and vaccine adjuvants.
Keywords: innate immunity, innate sensors, sugar associated PAMPs, disease pathogenesis, vaccinology
Citation: Mahla RS, Reddy MC, Prasad DVR and Kumar H (2013) Sweeten PAMPs: role of sugar complexed PAMPs in innate immunity and vaccine biology. Front. Immunol. 4:248. doi: 10.3389/fimmu.2013.00248
Received: 09 July 2013; Accepted: 09 August 2013;
Published online: 02 September 2013.
Edited by:Paul A. Ramsland, Burnet Institute, Australia
Reviewed by:Ashley Mansell, Monash Institute of Medical Research, Australia
Bernd Lepenies, Max Planck Society, Germany
Copyright: © 2013 Mahla, Reddy, Prasad and Kumar. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
*Correspondence: Himanshu Kumar, Laboratory of Immunology, Department of Biological Sciences, Indian Institute of Science Education and Research (IISER), Indore By-pass Road, Bhauri, Bhopal 462030, Madhya Pradesh, India e-mail: email@example.com