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A folding variant o...
A folding variant of alpha-lactalbumin with bactericidal activity against Streptococcus pneumoniae
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- Håkansson, Anders P (author)
- Lund University,Lunds universitet,Avdelningen för mikrobiologi, immunologi och glykobiologi - MIG,Institutionen för laboratoriemedicin,Medicinska fakulteten,Division of Microbiology, Immunology and Glycobiology - MIG,Department of Laboratory Medicine,Faculty of Medicine
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- Svensson, Malin (author)
- Lund University,Lunds universitet,Avdelningen för mikrobiologi, immunologi och glykobiologi - MIG,Institutionen för laboratoriemedicin,Medicinska fakulteten,Division of Microbiology, Immunology and Glycobiology - MIG,Department of Laboratory Medicine,Faculty of Medicine
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- Mossberg, A K (author)
- Lund University,Lunds universitet,Experimentell infektionsmedicin, Malmö,Forskargrupper vid Lunds universitet,Experimental Infection Medicine, Malmö,Lund University Research Groups
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Sabharwal, H (author)
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Linse, S (author)
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Lazou, I (author)
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Lönnerdal, B (author)
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- Svanborg, C (author)
- Lund University,Lunds universitet,Avdelningen för mikrobiologi, immunologi och glykobiologi - MIG,Institutionen för laboratoriemedicin,Medicinska fakulteten,Division of Microbiology, Immunology and Glycobiology - MIG,Department of Laboratory Medicine,Faculty of Medicine
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(creator_code:org_t)
- 2002-04-05
- 2000
- English 12 s.
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In: Molecular Microbiology. - : Wiley. - 0950-382X .- 1365-2958. ; 35:3, s. 589-600
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Abstract
Subject headings
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- 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.
Subject headings
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Mikrobiologi inom det medicinska området (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Microbiology in the medical area (hsv//eng)
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
Publication and Content Type
- art (subject category)
- ref (subject category)
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