Identification of lactoferrin-binding proteins inStreptococcus dysgalactiaesubsp.dysgalactiaeandStreptococcus agalactiaeisolated from cows with mastitis

Abstract

Three strains of Streptococcus dysgalactiae subsp. dysgalactiae (S. dysgalactiae) and five strains of Streptococcus agalactiae were used to identify lactoferrin-binding proteins (LBPs). LBPs from extracted surface proteins were detected by polyacrylamide gel electrophoresis and Western blotting. All strains of S. dysgalactiae evaluated had 52- and 74-kDa protein bands. All strains of S. agalactiae evaluated had 52-, 70- and 110-kDa protein bands. In addition, a 45-kDa band was detected in two of five S. agalactiae strains evaluated. This study demonstrated that S. dysgalactiae and S. agalactiae of bovine origin contain two and three major LBPs, respectively.

Exploring the mechanisms by which camel lactoferrin can kill Salmonella enterica serovar typhimurium and Shigella sonnei

“…Also, iron saturation of Lf can reverse this bacteriostatic effect in vivo ( Jahani, Shakiba & Jahani, 2015 ; Kell, Heyden & Pretorius, 2020 ). Our results showing cLf binding to bacterial membrane proteins of S. typhimurium and S. sonnei also support and agree with the previous reports on different bacterial strains, which demonstrated the presence of multiple and different lactoferrin-binding bacterial membrane proteins ( Drago-Serrano et al, 2010 ; Drago-Serrano et al, 2017 ; Schryvers & Morris, 1988 ; Staggs et al, 1994 ; Dhaenens, Szczebara & Husson, 1997 ; Tomita et al, 1998 ; Fang & Oliver, 1999 ; Park, Almeida & Oliver, 2002 ; Yu & Schryvers, 2002 ; Ochoa & Cleary, 2009 ; Rahman et al, 2009 ; Beddek & Schryvers, 2010 ; Morgenthau et al, 2014 ; Samaniego-Barrón et al, 2016 ).…”

Mini Review: Lactoferrin-binding protein of Streptococcus in Bovine Mastitis

“…Streptococcus is believed to be more insusceptible to the antimicrobial effects of lactoferrin since it has a minimum necessity of iron [38,39] or maybe due to the ability to extort the metal component other protein comprising iron [40]. Undeniably, several species of streptococcus express the lactoferrin-binding proteins, i.e., S. uberis, S. agalactiae, and S. dysgalactiae, implying an objective of lactoferrin with streptococcal infections which may have a crucial indication for Intra Mammary dysgalactiae streptolysin S, glyceraldehyde-3phosphate dehydrogenase, the plasminogen-binding Mlike protein PAM, and the collagen-like protein SclB, GAS bacteriophage-associated virulence genes encoding superantigens, DNase, and/or streptodornase, cfb, lmb, eno, napr, bca, scpB, cyl [32,33] uberis hasA, hasB, hasC, sua, gapC, lbp, pauA, oppF, mtuA, CAMP factor or cfu [34,35] Infection (IMI) pathogenesis [10]. However, there is a distinction in lactoferrin-binding protein molecular mass among streptococcus due to the diversity of their surface characteristic [41].…”

“…Meanwhile, the study by [44] points that bovine lactoferrin connects with S. agalactiae by the definite reciprocal action of lactoferrin with the bacterial surface which may have crucial consequences associated to host defense or the virulence of bacteria. Also, a study of the binding between bovine lactoferrinbinding protein and S. dysgalactiae taken by [10] exposed S. dysgalactiae is binding to lactoferrin and was not interrupted by molecule components of lactoferrin such as mannose, galactose, and lactose. The lactoferrin-binding protein is conveyed by S. agalactiae and S. dysgalactiae [10].…”

“…Also, a study of the binding between bovine lactoferrinbinding protein and S. dysgalactiae taken by [10] exposed S. dysgalactiae is binding to lactoferrin and was not interrupted by molecule components of lactoferrin such as mannose, galactose, and lactose. The lactoferrin-binding protein is conveyed by S. agalactiae and S. dysgalactiae [10]. The Study by [6] revealed that bovine intramammary is challenged with S. dysgalactiae significantly increase in milk lactoferrin protein compared with control.…”

“…Lactoferrin is a host innate immune protein that acts as antibacterial, immunomodulator, antiadhesion, and has iron-binding properties [7,8,9]. On the other hand, the LBP on the surface of Streptococcus could bind to lactoferrin produced by host cells [10]. Uniquely, a previous study revealed that the three Streptococcus…”