Thermal unfolding of human lysozyme induces aggregation: Recognition of the aggregates by antisera against the native protein

Md Tauqir Alam; Asim Rizvi; Mohd Ahmar Rauf; Mohammad Owais; Aabgeena Naeem

doi:10.1016/j.ijbiomac.2018.02.095

Thermal unfolding of human lysozyme induces aggregation: Recognition of the aggregates by antisera against the native protein

Int J Biol Macromol. 2018 Jul 1:113:976-982. doi: 10.1016/j.ijbiomac.2018.02.095. Epub 2018 Feb 17.

Authors

Md Tauqir Alam¹, Asim Rizvi¹, Mohd Ahmar Rauf², Mohammad Owais², Aabgeena Naeem³

Affiliations

¹ Department of Biochemistry, Faculty of Life Sciences, Aligarh Muslim University, Aligarh 202002, India.
² Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh 202002, India.
³ Department of Biochemistry, Faculty of Life Sciences, Aligarh Muslim University, Aligarh 202002, India. Electronic address: anaeem.bc@amu.ac.in.

PMID: 29462680
DOI: 10.1016/j.ijbiomac.2018.02.095

Abstract

Protein aggregates are formed due to the inappropriate folding of polypeptides. Human lysozyme (HLZ) plays an important role in the innate immune response of the body and has been used extensively as a model protein to study aggregation. In this study, we showed that HLZ undergoes unfolding induced aggregation when heated by using spectroscopic and microscopic techniques. We further showed that the aggregates were recognized by polyclonal antibodies against the native HLZ. The consequences of these observations are further co-related with mammalian physiology.

Keywords: Aggregation; ELISA; Human lysozyme (HLZ); Polyclonal antibodies; Western blot.

MeSH terms

Humans
Immune Sera / immunology*
Models, Molecular
Muramidase / chemistry*
Muramidase / immunology*
Protein Aggregates*
Protein Structure, Secondary
Protein Unfolding*
Temperature*

Substances

Immune Sera
Protein Aggregates
Muramidase