Apo-Lactoferrin Inhibits the Proteolytic Activity of the 110 KDa Zn Metalloprotease Produced by A2

Overview

Journal Int J Mol Sci

Publisher MDPI

Specialties Biochemistry
Chemistry
Molecular Biology

Date 2024 Aug 10

PMID 39125801

Authors

Gerardo Ramirez-Rico

Lucero Ruiz-Mazon

Magda Reyes-Lopez

Lina Rivillas Acevedo

Jesus Serrano-Luna

Mireya de la Garza

Affiliations

Soon will be listed here.

Abstract

is the main etiological bacterial agent in ruminant respiratory disease. secretes leukotoxin, lipopolysaccharides, and proteases, which may be targeted to treat infections. We recently reported the purification and in vivo detection of a 110 kDa Zn metalloprotease with collagenase activity (110-Mh metalloprotease) in a sheep with mannheimiosis, and this protease may be an important virulence factor. Due to the increase in the number of multidrug-resistant strains of , new alternatives to antibiotics are being explored; one option is lactoferrin (Lf), which is a multifunctional iron-binding glycoprotein from the innate immune system of mammals. Bovine apo-lactoferrin (apo-bLf) possesses many properties, and its bactericidal and bacteriostatic effects have been highlighted. The present study was conducted to investigate whether apo-bLf inhibits the secretion and proteolytic activity of the 110-Mh metalloprotease. This enzyme was purified and sublethal doses of apo-bLf were added to cultures of or co-incubated with the 110-Mh metalloprotease. The collagenase activity was evaluated using zymography and azocoll assays. Our results showed that apo-bLf inhibited the secretion and activity of the 110-Mh metalloprotease. Molecular docking and overlay assays showed that apo-bLf bound near the active site of the 110-Mh metalloprotease, which affected its enzymatic activity.

Citing Articles

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Kaplan M, Baktiroglu M, Kalkan A, Canbolat A, Lombardo M, Raposo A Nutrients. 2024; 16(18).

PMID: 39339673 PMC: 11435110. DOI: 10.3390/nu16183073.

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