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Agaricus bisporus mannose binding protein is not an agglutinating protein.

Authors :
Nabila, Najwa
Meidianto, Vincencius F.
Tjandrawinata, Raymond R.
Rachmawati, Heni
Ismaya, Wangsa T.
Source :
Biochemical & Biophysical Research Communications. Nov2019, Vol. 519 Issue 4, p773-776. 4p.
Publication Year :
2019

Abstract

Agaricus bisporus mannose binding protein (Abmb) demonstrates permeability to epithelial monolayer barrier of the intestine, resistance to gastrointestinal tract conditions and to proteolysis therefore it holds potential as a drug carrier for oral route administration. Abmb also display antiproliferative activity to breast cancer cells and stimulation of immune system thus could potentially be also developed for therapeutic purpose. It is not immunogenic or toxic thereby safe for use. In this paper we further provide evidence that Abmb also lacks of agglutinating activity despite sharing high structural homology to lectins. Abmb is thereby the only mannose specific binding protein that is not member of lectin family. This evidence provides further support on the use of Abmb as pharmaceutical or medicinal agent. Its molecular globularity that may contribute to its lack of agglutination capacity was also evaluated. • Abmb shares high structural homology to lectins. • Abmb has no agglutinating activity hence is not lectin. • Abmb is the only mannose binding protein that is not of lectin family. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
0006291X
Volume :
519
Issue :
4
Database :
Academic Search Index
Journal :
Biochemical & Biophysical Research Communications
Publication Type :
Academic Journal
Accession number :
139142051
Full Text :
https://doi.org/10.1016/j.bbrc.2019.09.071