Abstract:
:Lectins are a group of widely distributed and structurally heterogeneous proteins of nonimmune origin. These proteins have the ability to interact with glycans present on cell surfaces and elicit diverse biological activities. Machaerium acutifolium lectin (MaL) is an N-acetyl-D-glucosamine-binding lectin that exhibits antinociceptive activity via transient receptor potential cation channel subfamily V member 1 (TRPV1). Lectins that have the ability to recognize and interact with N-acetyl-D-glucosamine residues are potential candidates for studies of fungicidal activity. In this work, we show that MaL has antifungal activity against Candida species, and we describe its mode of action towards Candida parapsilosis. MaL inhibited the growth of C. albicans and C. parapsilosis. However, MaL was more potent against C. parapsilosis. The candidacidal mode of action of MaL on C. parapsilosis involves enhanced cell permeabilization, alteration of the plasma membrane proton-pumping ATPase function (H+-ATPase), induction of oxidative stress, and DNA damage. MaL also exhibited antibiofilm activity and noncytotoxicity to Vero cells. These results indicate that MaL is a promising candidate for the future development of a new, natural, and safe drug for the treatment of infections caused by C. parapsilosis.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Dias LP,Santos ALE,Araújo NMS,Silva RRS,Santos MHC,Roma RR,Rocha BAM,Oliveira JTA,Teixeira CSdoi
10.1016/j.ijbiomac.2020.06.236subject
Has Abstractpub_date
2020-11-15 00:00:00pages
19-25eissn
0141-8130issn
1879-0003pii
S0141-8130(20)33690-4journal_volume
163pub_type
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