Relationship between antibacterial activity and porin binding of lactoferrin in Escherichia coli and Salmonella typhimurium

Naidu, Sridevi; Svensson, Ulla; Kishore, A R; Naidu, A. S.

doi:10.1128/aac.37.2.240

Cited by 78 publications

(53 citation statements)

References 40 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Lf is also capable of causing cell membrane destruction by binding bacterial cell membrane proteins (24,25). Furthermore, it has an inhibitory effect on LPS-induced production of inflammatory cytokines (TNF-α, IL-1β, IL-6, and IL-8 mRNA) and in monocytic cells by interfering with NF-κB activation (26,27).…”

Section: Discussionmentioning

confidence: 99%

Influence of lactoferrin in preventing preterm delivery: A pilot study

Giunta¹,

Giuffrida²,

Mangano

et al. 2011

Mol Med Report

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 99%

Influence of lactoferrin in preventing preterm delivery: A pilot study

Giunta¹,

Giuffrida²,

Mangano

et al. 2011

Mol Med Report

View full text Add to dashboard Cite

“…Lactoferrin binds to Salmonella typhimurium [32]. Bovine lactoferrin (10e20% iron saturated) has an iron-dependent bacteriostatic effect on Salmonella typhimurium [33].…”

Section: Salmonellamentioning

confidence: 99%

Effect of lactoferrin on enteric pathogens

Ochoa

Cleary²

2009

Biochimie

118

View full text Add to dashboard Cite

Much has been learned in recent years about the mechanisms by which breastfeeding improves child health and survival. However, there has been little progress in using these insights to improve pediatric care. Factors that are important for protecting the breast fed infant might be expected to decrease the adverse effects of weaning on diarrhea, growth, and development. Lactoferrin, an ironbinding protein with multiple physiological functions (anti-microbial, anti-inflammatory, and immunomodulatory), is one of the most important proteins present in mammalian milk. Protection against gastroenteritis is the most likely biologically relevant activity of lactoferrin. Multiple in vitro and animal studies have shown a protective effect of lactoferrin on infections with enteric microorganisms, including rotavirus, Giardia, Shigella, Salmonella and the diarrheagenic Escherichia coli. Lactoferrin has two major effects on enteric pathogens: it inhibits growth and it impairs function of surface expressed virulence factors thereby decreasing their ability to adhere or to invade mammalian cells. Thus, lactoferrin may protect infants from gastrointestinal infection by preventing the attachment by enteropathogens in the gut. Recently several clinical trials in children have started to address this issue. Whether lactoferrin can prevent a significant portion of diarrheal disease remains to be determined.

show abstract

“…In Gram-negative bacteria, destabilization could partly be due to its binding capacity to lipid A and porins (3,4,10,25,37). Binding to lipopolysaccharide (LPS) has been suggested to release LPS from the bacterial membrane.…”

mentioning

confidence: 99%

Structure-Microbicidal Activity Relationship of Synthetic Fragments Derived from the Antibacterial α-Helix of Human Lactoferrin

Håversen

Kondori²,

Baltzer

et al. 2010

Antimicrob Agents Chemother

View full text Add to dashboard Cite

There is a need for new microbicidal agents with therapeutic potential due to antibiotic resistance in bacteria and fungi. In this study, the structure-microbicidal activity relationship of amino acid residues 14 to 31 (sequence 14-31) from the N-terminal end, corresponding to the antibacterial ␣-helix of human lactoferrin (LF), was investigated by downsizing, alanine scanning, and substitution of amino acids. Microbicidal analysis (99% killing) was performed by a microplate assay using Escherichia coli, Staphylococcus aureus, and Candida albicans as test organisms. Starting from the N-terminal end, downsizing of peptide sequence 14-31 showed that the peptide sequence 19-31 (KCFQWQRNMRKVR, HL9) was the optimal length for antimicrobial activity. Furthermore, HL9 bound to lipid A/lipopolysaccharide, as shown by neutralizing endotoxic activity in a Limulus assay. Alanine scanning of peptide sequence 20-31 showed that Cys20, Trp23, Arg28, Lys29, or Arg31 was important for expressing full killing activity, particularly against C. albicans. Substituting the neutral hydrophilic amino acids Gln24 and Asn26 for Lys and Ala (HLopt2), respectively, enhanced microbicidal activity significantly against all test organisms compared to the amino acids natural counterpart, also, in comparison with HL9, HLopt2 had more than 10-fold-stronger fungicidal activity. Furthermore, HLopt2 was less affected by metallic salts than HL9. The microbicidal activity of HLopt2 was slightly reduced only at pH 7.0, as tested in the pH range of 4.5 to 7.5. The results showed that the microbicidal activity of synthetic peptide sequences, based on the antimicrobial ␣-helix region of LF, can be significantly enhanced by optimizing the length and substitution of neutral amino acids at specific positions, thus suggesting a sequence lead with therapeutic potential.

show abstract

Relationship between antibacterial activity and porin binding of lactoferrin in Escherichia coli and Salmonella typhimurium

Cited by 78 publications

References 40 publications

Influence of lactoferrin in preventing preterm delivery: A pilot study

Influence of lactoferrin in preventing preterm delivery: A pilot study

Effect of lactoferrin on enteric pathogens

Structure-Microbicidal Activity Relationship of Synthetic Fragments Derived from the Antibacterial α-Helix of Human Lactoferrin

Contact Info

Product

Resources

About