» Articles » PMID: 8332105

Killing of Candida Albicans by Lactoferricin B, a Potent Antimicrobial Peptide Derived from the N-terminal Region of Bovine Lactoferrin

Overview
Date 1993 May 1
PMID 8332105
Citations 47
Authors
Affiliations
Soon will be listed here.
Abstract

Candida albicans was found to be highly susceptible to inhibition and inactivation by lactoferricin B, a peptide produced by enzymatic cleavage of bovine lactoferrin. Effective concentrations of the peptide varied within the range of 18 to 150 micrograms/ml depending on the strain and the culture medium used. Its effect was lethal, causing a rapid loss of colony-forming capability. 14C-labeled lactoferricin B bound to C. albicans and the rate of binding appeared to be consistent with the rate of killing induced by the peptide. The extent of binding was diminished in the presence of Mg2+ or Ca2+ ions which acted to reduce its anticandidal effectiveness. Binding occurred optimally at pH 6.0 and killing was maximal near the same pH. Such evidence suggests the lethal effect of lactoferricin B results from its direct interaction with the cell surface. Cells exposed to lactoferricin B exhibited profound ultrastructural damage which appeared to reflect its induction of an autolytic response. These findings suggest that active peptides of lactoferrin could potentially contribute to the host defense against C. albicans.

Citing Articles

Screening sensibility and antifungal activity after topical application of a synthetic lactoferrin-derived antimicrobial peptide.

Brouwer C, Boekhout T, Alwasel S, Rahman M, Janga R, Welling M Am J Transl Res. 2024; 16(2):669-680.

PMID: 38463589 PMC: 10918136.


Milk Antiviral Proteins and Derived Peptides against Zoonoses.

Santos I, Silva M, Gracio M, Pedroso L, Lima A Int J Mol Sci. 2024; 25(3).

PMID: 38339120 PMC: 10855762. DOI: 10.3390/ijms25031842.


Combining the Peptide RWQWRWQWR and an Ethanolic Extract of Enhances the Activity against Sensitive and Resistant and Strains.

Vargas-Casanova Y, Bravo-Chaucanes C, Martinez A, Costa G, Contreras-Herrera J, Medina R J Fungi (Basel). 2023; 9(8).

PMID: 37623588 PMC: 10455339. DOI: 10.3390/jof9080817.


A pilot study on ultrashort peptide with fluconazole: A promising novel anticandidal combination.

Darwish R, Salama A Vet World. 2023; 16(6):1284-1288.

PMID: 37577210 PMC: 10421555. DOI: 10.14202/vetworld.2023.1284-1288.


Time to Kill and Time to Heal: The Multifaceted Role of Lactoferrin and Lactoferricin in Host Defense.

Ohradanova-Repic A, Prazenicova R, Gebetsberger L, Moskalets T, Skrabana R, Cehlar O Pharmaceutics. 2023; 15(4).

PMID: 37111542 PMC: 10146187. DOI: 10.3390/pharmaceutics15041056.


References
1.
Epstein J, Truelove E, Izutzu K . Oral candidiasis: pathogenesis and host defense. Rev Infect Dis. 1984; 6(1):96-106. DOI: 10.1093/clinids/6.1.96. View

2.
BULLEN J . The significance of iron in infection. Rev Infect Dis. 1981; 3(6):1127-38. DOI: 10.1093/clinids/3.6.1127. View

3.
Bellamy W, Takase M, Yamauchi K, Wakabayashi H, Kawase K, Tomita M . Identification of the bactericidal domain of lactoferrin. Biochim Biophys Acta. 1992; 1121(1-2):130-6. DOI: 10.1016/0167-4838(92)90346-f. View

4.
Shepherd M, Poulter R, Sullivan P . Candida albicans: biology, genetics, and pathogenicity. Annu Rev Microbiol. 1985; 39:579-614. DOI: 10.1146/annurev.mi.39.100185.003051. View

5.
Xu T, Levitz S, DIAMOND R, Oppenheim F . Anticandidal activity of major human salivary histatins. Infect Immun. 1991; 59(8):2549-54. PMC: 258054. DOI: 10.1128/iai.59.8.2549-2554.1991. View