Antibacterial peptides of bovine lactoferrin: purification and characterization.
Open accessAbstract
Three peptides with antibacterial activity toward enterotoxigenic Escherichia coli have been purified from a pepsin digest of bovine lactoferrin. All peptides were cationic and originated from the N-terminus of the molecule in a region where a bactericidal peptide, lactoferricin B, had been previously identified. The most potent peptide, peptide I, was almost identical to lactoferricin B; the sequence corresponded to residues 17 to 42, and the molecular mass was 3195 as determined by mass spectrometry. A second, less active peptide, peptide II, consisted of two sequences, residues 1 to 16 and 43 to 48 (molecular mass of 2673), linked by a single disulfide bond. The third peptide, peptide III, also a disulfide-linked heterodimer, corresponded to residues 1 to 48 (molecular mass of 5851), cleaved between residues 42 and 43. Peptides I and II displayed antibacterial activity toward a number of pathogenic and food spoilage microorganisms, and peptide I inhibited the growth of Listeria monocytogenes at concentrations as low as 2 microM. Bacterial growth curves showed that bactericidal effects of peptides I and II were observable within 30 min of exposure. The results confirmed and extended those of earlier studies suggesting that the bactericidal domain of lactoferrin was localized in the N-terminus and did not involve iron-binding sites.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Lactoferricin B, having broad spectrum of action including Gram-negative and Gram-positive bacteria, yeasts and filamentous fungi, has been described as the result of hydrolytic action on bovine lactoferrin.
“An interesting antimicrobial peptide, named Lactoferricin B, having broad spectrum of action including Gram-negative and Gram-positive bacteria, yeasts and filamentous fungi, has been described as the result of the hydrolytic action on bovine lactoferrin (Dionysius and Milne, 1997; Kitts and Weiler, 2003).”
From Bioactive Molecules Released in Food by Lactic Acid Bacteria: Encrypted Peptides and Biogenic Amines (2016) · cites this paper as Dionysius and Milne, 1997
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Weinberg, E. D. (1978) · Microbiological Reviews · doi:10.1128/mmbr.42.1.45-66.1978 · Cited by 1,254 · see citing works
Molecular basis of bacterial outer membrane permeability.
Nikaido, H., & Vaara, M. (1985) · Microbiological Reviews · doi:10.1128/mmbr.49.1.1-32.1985 · Cited by 907 · see citing works
Identification of the bactericidal domain of lactoferrin
Bellamy, W., Takase, M., Yamauchi, K., Wakabayashi, H., Kawase, K., & TOMITA, M. (1992) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(92)90346-f · Cited by 890 · see citing works
A Bactericidal Effect for Human Lactoferrin
Arnold, R. R., Cole, M. F., & McGhee, J. R. (1977) · Science · doi:10.1126/science.327545 · Cited by 677 · see citing works
Iron-binding Proteins in Milk and Resistance to Escherichia coli Infection in Infants
Bullen, J. J., Rogers, H. J., & Leigh, L. C. (1972) · BMJ · doi:10.1136/bmj.1.5792.69 · Cited by 651 · see citing works
Bellamy, W., Takase, M., Wakabayashi, H., Kawase, K., & TOMITA, M. (1992) · Journal of Applied Bacteriology · doi:10.1111/j.1365-2672.1992.tb05007.x · Cited by 588 · see citing works
An iron-binding protein common to many external secretions
Masson, P. L., Heremans, J. F., & Dive, C. H. (1966) · Clinica Chimica Acta · doi:10.1016/0009-8981(66)90004-0 · Cited by 577 · see citing works
Molecular basis of bacterial outer membrane permeability
Nikaido, H., & Vaara, M. (1985) · Microbiological Reviews · doi:10.1128/mr.49.1.1-32.1985 · Cited by 553 · see citing works
Damage of the outer membrane of enteric gram-negative bacteria by lactoferrin and transferrin
Ellison, R. T., Giehl, T. J., & LaForce, F. M. (1988) · Infection and Immunity · doi:10.1128/iai.56.11.2774-2781.1988 · Cited by 540 · see citing works
Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment
Yamauchi, K., Tomita, M., Giehl, T. J., & Ellison, R. T. (1993) · Infection and Immunity · doi:10.1128/iai.61.2.719-728.1993 · Cited by 500 · see citing works
Potent Antibacterial Peptides Generated by Pepsin Digestion of Bovine Lactoferrin
TOMITA, M., Bellamy, W., Takase, M., Yamauchi, K., Wakabayashi, H., & Kawase, K. (1991) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(91)78608-6 · Cited by 445 · see citing works
Apolactoferrin structure demonstrates ligand-induced conformational change in transferrins
Andersen, B. F., Baker, H. M., Morris, G. E., Rumball, S. V., & Baker, E. N. (1990) · Nature · doi:10.1038/344784a0 · Cited by 363 · see citing works
ASSOCIATION OF LACTOFERRIN WITH SPECIFIC GRANULES IN RABBIT HETEROPHIL LEUKOCYTES
Baggiolini, M., Duve, C. D., Masson, P. L., & Heremans, J. F. (1970) · The Journal of Experimental Medicine · doi:10.1084/jem.131.3.559 · Cited by 269 · see citing works
Molecular cloning and sequence analysis of bovine lactotransferrin
Pierce, A., Colavizza, D., Benaı̈ssa, M., Mäes, P., Tartar, A. L., Montreuil, J., & Spik, G. (1991) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1991.tb15801.x · Cited by 253 · see citing works
A review: The active peptide of lactoferrin
TOMITA, M., Takase, M., Bellamy, W., & Shimamura, S. (1994) · Pediatrics International · doi:10.1111/j.1442-200x.1994.tb03250.x · Cited by 180 · see citing works
The isolation and bacteriostatic properties of lactoferrin from bovine milk whey
Law, B. A., & Reiter, B. (1977) · Journal of Dairy Research · doi:10.1017/s0022029900020550 · Cited by 139 · see citing works
Concentration of Lactoferrin and Transferrin throughout Lactation in Cow’s Colostrum and Milk
Sánchez, L., Aranda, P., Pérez, M. D., & Calvo, M. (1988) · Biological Chemistry Hoppe-Seyler · doi:10.1515/bchm3.1988.369.2.1005 · Cited by 121 · see citing works
Bishop, J., Schanbacher, F. L., Ferguson, L. C., & Smith, K. L. (1976) · Infection and Immunity · doi:10.1128/iai.14.4.911-918.1976 · Cited by 105 · see citing works
Bovine lactoferrin mRNA: Sequence, analysis, and expression in the mammary gland
Goodman, R. E., & Schanbacher, F. L. (1991) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(05)81257-4 · Cited by 105 · see citing works
Role of cell-binding in the antibacterial mechanism of lactoferricin B.
Bellamy, W., Wakabayashi, H., Takase, M., Kawase, K., Shimamura, S., & Tomita, M. (1993) · PubMed · Cited by 90 · see citing works
Forms of Lactoferrin: Their Antibacterial Effect on Enterotoxigenic Escherichia coli
Dionysius, D. A., Grieve, P. A., & Milne, J. M. (1993) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(93)77594-3 · Cited by 86 · see citing works
Self-citationNaidu, S. S., Svensson, U., Kishore, A. R., et al. (1993) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.37.2.240 · Cited by 83 · see citing works
Nonnecke, B. J., & Smith, K. L. (1984) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(84)81345-4 · Cited by 67 · see citing works
Enhanced antimicrobial activity of lactoferrin by binding to the bacterial surface.
Dalmastri, C., Valenti, P., Visca, P., Vittorioso, P., & Orsi, N. (1988) · PubMed · Cited by 63 · see citing works
Legrand, D., Mazurier, J., Colavizza, D., et al. (1990) · PubMed · Cited by 61 · see citing works
THE INFLUENCE OF DISTILLED WATER ON THE HEALING OF SKIN WOUNDS IN THE FROG
Ruth, E. S. (1911) · The Journal of Experimental Medicine · doi:10.1084/jem.13.5.559 · Cited by 15 · see citing works
Enhancement of the activity of cefotaxime by iron-binding proteins
Ellison, R. T., LUO, Q., & Reller, L. B. (1990) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/25.3.479 · Cited by 9 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Bioactive Molecules Released in Food by Lactic Acid Bacteria: Encrypted Peptides and Biogenic Amines
Pessione, E., & Cirrincione, S. (2016) · Frontiers in Microbiology · doi:10.3389/fmicb.2016.00876 · Cited by 333 · see citing works
Meisel, H., & Bockelmann, W. (1999) · Antonie van Leeuwenhoek · doi:10.1023/a:1002063805780 · Cited by 284 · see citing works
Angiotensin I-converting-enzyme-inhibitory and antimicrobial bioactive peptides.
Gobbetti, M., Minervini, F., & Rizzello, C. G. (2004) · International Journal of Dairy Technology · doi:10.1111/j.1471-0307.2004.00139.x · Cited by 268 · see citing works
Lactoferrin: a multifunctional glycoprotein.
Vorland, L. H. (1999) · APMIS · doi:10.1111/j.1699-0463.1999.tb01499.x · Cited by 252 · see citing works
Bioactive peptides from milk: Animal determinants and their implications in human health
Vargas-Bello-Pérez, E., Márquez-Hernández, R. I., & Hernández-Castellano, L. E. (2019) · Journal of Dairy Research · doi:10.1017/s0022029919000384 · Cited by 97 · see citing works
Discovery and development of a synthetic peptide derived from lactoferrin for clinical use
Brouwer, C. P. J. M., Rahman, M., & Welling, M. M. (2011) · Peptides · doi:10.1016/j.peptides.2011.07.017 · Cited by 90 · see citing works
Diarra, M. S., Petitclerc, D., & Lacasse, P. (2002) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(02)74176-3 · Cited by 86 · see citing works
Roy, M. K., Kuwabara, Y., Hara, K., Watanabe, Y., & Tamai, Y. (2002) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(02)74284-7 · Cited by 74 · see citing works
Roy, M. K., Watanabe, Y., & Tamai, Y. (1999) · Journal of Bioscience and Bioengineering · doi:10.1016/s1389-1723(99)80221-7 · Cited by 33 · see citing works
- Authors
- Dionysius, D. A., & Milne, J. M.
- Affiliations
- Department of Primary Industries (AU)
- Venue
- Journal of Dairy Science
- Publisher
- American Dairy Science Association
- Published
- 1997-04
- Volume
- 80
- Issue
- 4
- Pages
- 667-674
- ISSN
- 0022-0302 (ISSN-L)
- OpenAlex
- W2069928195
- Cited by
- 166
- References
- 27
- Citations by year
- 2026: 3 · 2025: 3 · 2024: 4 · 2023: 5 · 2022: 4 · 2021: 1 · 2019: 4 · 2018: 2 · 2017: 2 · 2016: 4 · 2015: 4 · 2014: 4 · 2013: 4 · 2012: 7
- FWCI
- 7.70
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Journal of Dairy Science (publishedVersion)
- PubMed (publishedVersion)
- Queensland Department of Agriculture and Fisheries archive of scientific and research publications (Queensland Department of Agriculture and Fisheries) (submittedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Hydrolysis and Bioactive Peptides
- Health Sciences › Nursing › Nutrition and Dietetics › Infant Nutrition and Health
- Keywords
- bovine lactoferrin, antibacterial peptides, lactoferricin B, enterotoxigenic Escherichia coli, Listeria monocytogenes, bactericidal activity, disulfide-linked heterodimer, cationic peptides, spoilage microorganisms, pepsin digestion, peptide purification
- MeSH terms
- Amino Acid Sequence, Animals, Cattle, Chromatography, High Pressure Liquid, Electrophoresis, Polyacrylamide Gel, Escherichia coli, Lactoferrin, Listeria monocytogenes, Molecular Sequence Data, Peptides, Mass Spectrometry, Time Factors
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
