Journal of Clinical and Cellular Immunology
Open Access

Characterisation of collections CL-Kl and CL-L1 and their role in the innate immune response

10^th World Congress and Expo on Immunology, Immunity, Inflammation & Immunotherapies

October 19-20, 2018 | New York, USA

Luay AL-Kanan

University of Leicester, United Kingdom

Posters & Accepted Abstracts: J Clin Cell Immunol

Abstract :

The immune system is a collection of proteins, cells and other biological components that protect an organism against pathogenic microbes. It prevents an attack through a series of processes collectively called the immune response. The complement system is an essential part of the innate immune response. Complement is activated by three pathways: the Classical (CP), the Lectin (LP) and the Alternative pathways (AP). The LP is activated by a range of different pathogenrecognition receptors including collecting kidney-1 (CL-K1 aka CL-11) and collecting liver-1 (CL-L1 aka CL-10), which bind to pathogen-associated molecular patterns (PAMPs), to activate three MBL-associated serine proteases (MASPs). CL-K1 and CL-L1 play an important role in host defense by recognizing a range of pathogens. These proteins can activate the LP individually or as a hetero-oligomeric complex. The sugar specificity of CL-K1 has been analyzed recently, it binds to highmannose type structures and a range of different fucose-containing sugars including Lewis antigens and Blood group antigens. Binding of the former have been characterized structurally but binding to fucose-containing structures has not. In addition, the sugar specificities of CL-L1 is unknown. Here we present structures highlighting the ligand binding by CL-L1 and CL-K1. CL-K1 is known to bind to mannose and fucose-containing sugars, which are commonly found on bacterial surfaces.

Biography :

Luay AL-Kanan PhD student working with Professor Wallis group in molecular biology and complement related disease.

E-mail: lhaak2@le.ac.uk