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Cited by 119Antimicrobial Peptides and ActivitiesProtein Hydrolysis and Bioactive PeptidesAntimicrobial agents and applications

The DOI matches its Crossref record; 40 of the 40 references it cites were found in a registry or an index.

Identification of a distinct antibacterial domain within the N-lobe of ovotransferrin

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Ibrahim, Hisham R, Iwamori, Eiko, Sugimoto, Yasushi, Aoki, Takayoshi·1998·Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
DOI 10.1016/s0167-4889(97)00132-8
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Abstract

We have evaluated the bactericidal activity of hen ovotransferrin (OTf), which was found to operate regardless of its iron-deprivation properties, with the objective of isolating the bactericidal domain. The amino-terminal half-molecule (N-lobe, residues 1-332) of OTf, isolated by trypsin-nicking, retained the bactericidal activity independently of iron-deprivation, but not the carboxyl-terminal half-molecule (C-lobe, residue 342-686), suggesting the presence of a bactericidal domain within the N-lobe of the molecule. Specific cleavage at the aspartyl residues of OTf, by diluted-acid procedure, yielded fairly large peptides, whereas proteolysis for 150 min produced the strongest bactericidal peptides mixture. The bactericidal domain was purified from the active hydrolysate by gel filtration and reversed-phase HPLC and showed activity against S. aureus as well as E. coli K-12. Electrophoretic analysis on tricine-SDS-PAGE revealed a bactericidal peptide with an average M(r) of 9900 Da under non-reducing conditions. In combination with the specificity of cleavage (Asp-X) and the molecular mass, its N-terminal microsequencing corresponded to a cationic peptide consisting of 92 residues located within the 109-200 sequence of the N-lobe of OTf, containing three intrachain disulfide bridges, featuring a common structural motif occurs in the N-lobes of transferrins for which the sequence is available. Two of the disulfides (C160-C174 and C171-C182) form surface exposed cringle bridges lying on the opposite side of the iron-binding site from the interdomain cleft and showing marked sequence homology to insect defensins, which are blockers of the voltage-dependent K+ channels. The peptide lost antibacterial activity when its disulfide bonds were reduced, indicating the importance of its tertiary structure for the exertion of antibiotic activity.

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  • OTAP-92 is a large ovotransferrin-derived peptide with antibacterial activity and a membrane-damaging mechanism against bacteria.

    “Ibrahim and colleagues described OTAP-92, a large ovotransferrin-derived peptide with antibacterial activity and a membrane-damaging mechanism against bacteria [13,14].”

    From Ovotransferrin and Its γ-Core-Containing Peptides Impair Pma1-Dependent Proton Homeostasis in Candida albicans (2026) · cites this paper as [13]

    The Discussion identifies OTAP-92 as a 92-residue bactericidal domain from ovotransferrin and reports that it kills the tested bacteria. It does not establish a membrane-damaging mechanism; instead, it says further experiments are needed to study how OTAP-92 acts. (LLM, conf=0.88)

    Experimental — accuracy not yet measured

  • Kal-3 lies within OTAP-92, a cysteine-rich 92-residue N-lobe fragment containing three intrachain disulfide bonds, whose reduction abolished its antibacterial activity.

    “Kal-3 lies within OTAP-92, a cysteine-rich 92-residue N-lobe fragment containing three intrachain disulfide bonds, whose reduction abolished its antibacterial activity [13].”

    From Ovotransferrin and Its γ-Core-Containing Peptides Impair Pma1-Dependent Proton Homeostasis in Candida albicans (2026) · cites this paper as [13]

    The Discussion (p. 300) identifies OTAP-92 as a 92-residue N-lobe peptide with six cysteines forming three intrachain disulfide bridges. Section 3.3 reports that reducing those bridges completely abolished its bactericidal activity against the bacteria tested. Our copy does not identify Kal-3 or establish that it lies within OTAP-92. (LLM, conf=0.88)

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Research works printed but not linked: 2

  1. Bullen, 1978, Curr. Top. Microbiol. Immunol., 80, 1
  2. Valenti, 1983, Int. J. Tiss. Reac., 1, 97

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Metadata

Authors
Ibrahim, H. R., Iwamori, E., Sugimoto, Y., & Aoki, T.
Affiliations
Kagoshima University (JP)
Corresponding author
Ibrahim, Hisham R
ORCID
Venue
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
Publisher
Elsevier BV
Published
1998-03
Volume
1401
Issue
3
Pages
289-303
ISSN
0167-4889 (ISSN-L)
DOI
10.1016/s0167-4889(97)00132-8
OpenAlex
W2069770564
Semantic Scholar
9068c4690c11b48e09b8be2a6d5d393f10d4789b
Cited by
119
References
40
Citations by year
2026: 2 · 2024: 1 · 2022: 3 · 2021: 4 · 2020: 5 · 2019: 3 · 2017: 6 · 2016: 5 · 2015: 27 · 2014: 4 · 2013: 6 · 2012: 3
FWCI
1.08
Type
journal article
Language
en
Open access
Licence
Locations
  • Biochimica et Biophysica Acta (BBA) - Molecular Cell Research (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Protein Hydrolysis and Bioactive Peptides
  • Life Sciences › Immunology and Microbiology › Applied Microbiology and Biotechnology › Antimicrobial agents and applications
Keywords
ovotransferrin, bactericidal activity, antibacterial peptides, N-lobe, disulfide bonds, Staphylococcus aureus, Escherichia coli, iron binding sites, cationic peptides, peptide tertiary structure, egg yolk proteins
MeSH terms
Amino Acid Sequence, Animals, Aspartic Acid, Bacteria, Chickens, Chromatography, Gel, Chromatography, High Pressure Liquid, Conalbumin, Hydrochloric Acid, Iron, Microbial Sensitivity Tests, Molecular Sequence Data, Peptide Fragments, Protein Conformation, Structure-Activity Relationship, Sequence Homology, Amino Acid

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