Killing of Candida albicans by lactoferricin B, a potent antimicrobial peptide derived from the N-terminal region of bovine lactoferrin

1993 ◽  
Vol 182 (2) ◽  
Author(s):  
Wayne Bellamy ◽  
Hiroyuki Wakabayashi ◽  
Mitsunori Takase ◽  
Kouzou Kawase ◽  
Seiichi Shimamura ◽  
...  
Keyword(s):  
Candida Albicans ◽  
Antimicrobial Peptide ◽  
Terminal Region ◽  
Bovine Lactoferrin

Lactoferrampin, an antimicrobial peptide of bovine lactoferrin, exerts its candidacidal activity by a cluster of positively charged residues at the C-terminus in combination with a helix-facilitating N-terminal part

2005 ◽  
Vol 386 (2) ◽  
pp. 137-142 ◽  
Author(s):  
Marieke I.A. van der Kraan ◽  
Kamran Nazmi ◽  
Afke Teeken ◽  
Jasper Groenink ◽  
Wim van 't Hof ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Candida Albicans ◽  
Antimicrobial Peptide ◽  
Helical Conformation ◽  
Bovine Lactoferrin ◽  
Terminal Part ◽  
Helix Formation ◽  
C Terminus ◽  
Charged Residues ◽  
Positively Charged

AbstractThe antimicrobial activity of bovine lactoferrin (bLF) is attributed to lactoferricin, which is situated in the N1-domain of bLF. Recently, another antimicrobial domain consisting of residues 268–284, designated lactoferrampin (LFampin), has been identified in the N1-domain of bLF, which exhibited antimicrobial activity againstCandida albicansand several bacteria. In the present study, the candidacidal activity of a series of peptides spanning this antimicrobial domain was investigated in relation to the charge and the capacity to form a helical conformation in hydrophobic environments. C-Terminal truncation of LFampin resulted in a drastic decrease in candidacidal activity. Positively charged residues clustered at the C-terminal side of the LFampin domain appeared to be crucial for the candidacidal activity. The ability to adopt helical conformations did not change when LFampin was truncated at the C-terminal side. N-Terminally truncated LFampin peptides, truncated up to the sequence 270–284, were more reluctant to adopt a helical conformation. Therefore, we conclude that the C-terminal part of LFampin 265–284, which is the most active peptide, is crucial for its candidacidal activity, due to the presence of clustered positive charges, and that the N-terminal part is essential for activity as it facilitates helix formation.

Three-Dimensional Solution Structure of Lactoferricin B, an Antimicrobial Peptide Derived from Bovine Lactoferrin†

Biochemistry ◽  
1998 ◽  
Vol 37 (12) ◽  
pp. 4288-4298 ◽  
Author(s):  
Peter M. Hwang ◽  
Ning Zhou ◽  
Xi Shan ◽  
Cheryl H. Arrowsmith ◽  
Hans J. Vogel
Keyword(s):  
Antimicrobial Peptide ◽  
Solution Structure ◽  
Three Dimensional ◽  
Bovine Lactoferrin ◽  
Dimensional Solution

Antifungal properties of lactoferricin B, a peptide derived from the N-terminal region of bovine lactoferrin

1994 ◽  
Vol 18 (4) ◽  
pp. 230-233 ◽  
Author(s):  
W. Bellamy ◽  
K. Yamauchi ◽  
H. Wakabayashi ◽  
M. Takase ◽  
N. Takakura ◽  
...  
Keyword(s):  
Terminal Region ◽  
Bovine Lactoferrin ◽  
Antifungal Properties

scholarly journals SSD1 Is Integral to Host Defense Peptide Resistance in Candida albicans

2008 ◽  
Vol 7 (8) ◽  
pp. 1318-1327 ◽  
Author(s):  
Kimberly D. Gank ◽  
Michael R. Yeaman ◽  
Satoshi Kojima ◽  
Nannette Y. Yount ◽  
Hyunsook Park ◽  
...  
Keyword(s):  
Candida Albicans ◽  
Antimicrobial Peptides ◽  
Antimicrobial Peptide ◽  
Host Defense ◽  
Genomic Library ◽  
Inflammatory Responses ◽  
Host Defense Peptides ◽  
Antimicrobial Peptide Resistance ◽  
Null Mutants

ABSTRACT Candida albicans is usually a harmless human commensal. Because inflammatory responses are not normally induced by colonization, antimicrobial peptides are likely integral to first-line host defense against invasive candidiasis. Thus, C. albicans must have mechanisms to tolerate or circumvent molecular effectors of innate immunity and thereby colonize human tissues. Prior studies demonstrated that an antimicrobial peptide-resistant strain of C. albicans, 36082R, is hypervirulent in animal models versus its susceptible counterpart (36082S). The current study aimed to identify a genetic basis for antimicrobial peptide resistance in C. albicans. Screening of a C. albicans genomic library identified SSD1 as capable of conferring peptide resistance to a susceptible surrogate, Saccharomyces cerevisiae. Sequencing confirmed that the predicted translation products of 36082S and 36082R SSD1 genes were identical. However, Northern analyses corroborated that SSD1 is expressed at higher levels in 36082R than in 36082S. In isogenic backgrounds, ssd1Δ/ssd1Δ null mutants were significantly more susceptible to antimicrobial peptides than parental strains but had equivalent susceptibilities to nonpeptide stressors. Moreover, SSD1 complementation of ssd1Δ/ssd1Δ mutants restored parental antimicrobial peptide resistance phenotypes, and overexpression of SSD1 conferred enhanced peptide resistance. Consistent with these in vitro findings, ssd1 null mutants were significantly less virulent in a murine model of disseminated candidiasis than were their parental or complemented strains. Collectively, these results indicate that SSD1 is integral to C. albicans resistance to host defense peptides, a phenotype that appears to enhance the virulence of this organism in vivo.

scholarly journals Antimicrobial Peptide AMP-17 Affects Candida albicans by Disrupting Its Cell Wall and Cell Membrane Integrity

2020 ◽  
Vol Volume 13 ◽  
pp. 2509-2520
Author(s):  
Huiling Ma ◽  
Xinyu Zhao ◽  
Longbing Yang ◽  
Peipei Su ◽  
Ping Fu ◽  
...  
Keyword(s):  
Cell Wall ◽  
Candida Albicans ◽  
Cell Membrane ◽  
Antimicrobial Peptide ◽  
Membrane Integrity ◽  
Cell Membrane Integrity

Responses of Candida albicans to the human antimicrobial peptide LL-37

2014 ◽  
Vol 52 (7) ◽  
pp. 581-589 ◽  
Author(s):  
Pei-Wen Tsai ◽  
Yin-Lien Cheng ◽  
Wen-Ping Hsieh ◽  
Chung-Yu Lan
Keyword(s):  
Candida Albicans ◽  
Antimicrobial Peptide

scholarly journals TMT-based quantitative proteomic analysis of the effects of novel antimicrobial peptide AMP-17 against Candida albicans

2022 ◽  
Vol 250 ◽  
pp. 104385
Author(s):  
Long-Bing Yang ◽  
Guo Guo ◽  
Zhu-Qing Tian ◽  
Luo-Xiong Zhou ◽  
Li-Juan Zhu ◽  
...  
Keyword(s):  
Candida Albicans ◽  
Antimicrobial Peptide ◽  
Proteomic Analysis ◽  
Quantitative Proteomic Analysis

Lactoferrampin: a novel antimicrobial peptide in the N1-domain of bovine lactoferrin

Peptides ◽  
2004 ◽  
Vol 25 (2) ◽  
pp. 177-183 ◽  
Author(s):  
Marieke I.A van der Kraan ◽  
Jasper Groenink ◽  
Kamran Nazmi ◽  
Enno C.I Veerman ◽  
Jan G.M Bolscher ◽  
...  
Keyword(s):  
Antimicrobial Peptide ◽  
Bovine Lactoferrin
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