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A folding variant of alpha-lactalbumin with bactericidal activity against Streptococcus pneumoniae

Håkansson, Anders P LU ; Svensson, Malin LU ; Mossberg, A K LU ; Sabharwal, H; Linse, S LU ; Lazou, I; Lönnerdal, B and Svanborg, C LU (2000) In Molecular Microbiology 35(3). p.589-600
Abstract

This study describes an alpha-lactalbumin folding variant from human milk with bactericidal activity against antibiotic-resistant and -susceptible strains of Streptococcus pneumoniae. The active complex precipitated with the casein fraction at pH 4.6 and was purified from casein by a combination of anion exchange and gel chromatography. Unlike other casein components, the active complex was retained on the ion-exchange matrix and eluted only with high salt. The eluted fraction showed N-terminal and mass spectrometric identity with human milk alpha-lactalbumin, but native alpha-lactalbumin had no bactericidal effect. Spectroscopic analysis demonstrated that the active form of the molecule was in a different folding state, with secondary... (More)

This study describes an alpha-lactalbumin folding variant from human milk with bactericidal activity against antibiotic-resistant and -susceptible strains of Streptococcus pneumoniae. The active complex precipitated with the casein fraction at pH 4.6 and was purified from casein by a combination of anion exchange and gel chromatography. Unlike other casein components, the active complex was retained on the ion-exchange matrix and eluted only with high salt. The eluted fraction showed N-terminal and mass spectrometric identity with human milk alpha-lactalbumin, but native alpha-lactalbumin had no bactericidal effect. Spectroscopic analysis demonstrated that the active form of the molecule was in a different folding state, with secondary structure identical to alpha-lactalbumin from human milk whey, but fluctuating tertiary structure. Native alpha-lactalbumin could be converted to the active bactericidal form by ion-exchange chromatography in the presence of a cofactor from human milk casein, characterized as a C18:1 fatty acid. Analysis of the antibacterial spectrum showed selectivity for streptococci; Gram-negative and other Gram-positive bacteria were resistant. The folding variant of alpha-lactalbumin is a new example of naturally occurring molecules with antimicrobial activity.

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organization
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Contribution to journal
publication status
published
subject
keywords
Anti-Bacterial Agents, Caseins, Chemical Fractionation, Chromatography, Ion Exchange, Drug Resistance, Microbial, Fatty Acids, Humans, Lactalbumin, Mass Spectrometry, Microbial Sensitivity Tests, Milk, Human, Protein Folding, Sequence Analysis, Protein, Spectrum Analysis, Streptococcus pneumoniae
in
Molecular Microbiology
volume
35
issue
3
pages
12 pages
publisher
Wiley-Blackwell
external identifiers
  • scopus:0033950960
ISSN
0950-382X
DOI
10.1046/j.1365-2958.2000.01728.x
language
English
LU publication?
yes
id
c309d373-3073-42da-bf8b-56dc393bd192
date added to LUP
2016-05-21 11:23:28
date last changed
2017-04-30 17:19:49
@article{c309d373-3073-42da-bf8b-56dc393bd192,
  abstract     = {<p>This study describes an alpha-lactalbumin folding variant from human milk with bactericidal activity against antibiotic-resistant and -susceptible strains of Streptococcus pneumoniae. The active complex precipitated with the casein fraction at pH 4.6 and was purified from casein by a combination of anion exchange and gel chromatography. Unlike other casein components, the active complex was retained on the ion-exchange matrix and eluted only with high salt. The eluted fraction showed N-terminal and mass spectrometric identity with human milk alpha-lactalbumin, but native alpha-lactalbumin had no bactericidal effect. Spectroscopic analysis demonstrated that the active form of the molecule was in a different folding state, with secondary structure identical to alpha-lactalbumin from human milk whey, but fluctuating tertiary structure. Native alpha-lactalbumin could be converted to the active bactericidal form by ion-exchange chromatography in the presence of a cofactor from human milk casein, characterized as a C18:1 fatty acid. Analysis of the antibacterial spectrum showed selectivity for streptococci; Gram-negative and other Gram-positive bacteria were resistant. The folding variant of alpha-lactalbumin is a new example of naturally occurring molecules with antimicrobial activity.</p>},
  author       = {Håkansson, Anders P and Svensson, Malin and Mossberg, A K and Sabharwal, H and Linse, S and Lazou, I and Lönnerdal, B and Svanborg, C},
  issn         = {0950-382X},
  keyword      = {Anti-Bacterial Agents,Caseins,Chemical Fractionation,Chromatography, Ion Exchange,Drug Resistance, Microbial,Fatty Acids,Humans,Lactalbumin,Mass Spectrometry,Microbial Sensitivity Tests,Milk, Human,Protein Folding,Sequence Analysis, Protein,Spectrum Analysis,Streptococcus pneumoniae},
  language     = {eng},
  number       = {3},
  pages        = {589--600},
  publisher    = {Wiley-Blackwell},
  series       = {Molecular Microbiology},
  title        = {A folding variant of alpha-lactalbumin with bactericidal activity against Streptococcus pneumoniae},
  url          = {http://dx.doi.org/10.1046/j.1365-2958.2000.01728.x},
  volume       = {35},
  year         = {2000},
}