Open AccessCharacterisation of 20‐kDa lectin‐spermagglutinin from Arum maculatum that prevents Chlamydia pneumoniae infection of L‐929 fibroblast cells
Author(s) -
Mladenov Ivan V,
Haralambieva Iana H,
Iankov Ianko D,
Mitov Ivan G
Publication year - 2002
Publication title -
fems immunology & medical microbiology
Language(s) - English
Resource type - Journals
eISSN - 1574-695X
pISSN - 0928-8244
DOI - 10.1111/j.1574-695x.2002.tb00561.x
Subject(s) - lectin , sialoglycoprotein , biology , agglutinin , agglutination (biology) , fibroblast , microbiology and biotechnology , hemagglutination , biochemistry , percoll , mannan binding lectin , cell , antibody , in vitro , immunology
A novel lectin from the root of Arum maculatum was isolated by saline extraction and purified by cold ethanol precipitation and subsequent fractionation on Superose 6 column. The lectin named A. maculatum agglutinin is a non‐glycosylated protein with 20‐kDa molecular mass agglutinating human ejaculated spermatozoa, but not human erythrocytes. The agglutination was blocked in the presence of N ‐acetylneuraminic acid indicating that the lectin is sialoglycoprotein specific. Chlamydia pneumoniae strain AR‐39 showed considerable potential to grow in murine L‐929 fibroblast cells. Pretreatment of the cell monolayers with purified lectin reduced the entry and intracellular replication of C. pneumoniae . These results suggest that the isolated lectin prevents attachment by binding to a C. pneumoniae specific sialoglycoprotein receptor expressed on the surface of L‐929 fibroblast cells.