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Home / Equine Research Bank / J R Soc Interface / The structure of latherin, a surfactant allergen protein fro...
Journal of the Royal Society, Interface2013; 10(85); 20130453; doi: 10.1098/rsif.2013.0453

The structure of latherin, a surfactant allergen protein from horse sweat and saliva.

Abstract: Latherin is a highly surface-active allergen protein found in the sweat and saliva of horses and other equids. Its surfactant activity is intrinsic to the protein in its native form, and is manifest without associated lipids or glycosylation. Latherin probably functions as a wetting agent in evaporative cooling in horses, but it may also assist in mastication of fibrous food as well as inhibition of microbial biofilms. It is a member of the PLUNC family of proteins abundant in the oral cavity and saliva of mammals, one of which has also been shown to be a surfactant and capable of disrupting microbial biofilms. How these proteins work as surfactants while remaining soluble and cell membrane-compatible is not known. Nor have their structures previously been reported. We have used protein nuclear magnetic resonance spectroscopy to determine the conformation and dynamics of latherin in aqueous solution. The protein is a monomer in solution with a slightly curved cylindrical structure exhibiting a 'super-roll' motif comprising a four-stranded anti-parallel β-sheet and two opposing α-helices which twist along the long axis of the cylinder. One end of the molecule has prominent, flexible loops that contain a number of apolar amino acid side chains. This, together with previous biophysical observations, leads us to a plausible mechanism for surfactant activity in which the molecule is first localized to the non-polar interface via these loops, and then unfolds and flattens to expose its hydrophobic interior to the air or non-polar surface. Intrinsically surface-active proteins are relatively rare in nature, and this is the first structure of such a protein from mammals to be reported. Both its conformation and proposed method of action are different from other, non-mammalian surfactant proteins investigated so far.
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Publication Date: 2013-06-19 PubMed ID: 23782536PubMed Central: PMC4043175DOI: 10.1098/rsif.2013.0453Google Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This research paper investigates the structure and function of latherin, a protein found in horse sweat and saliva that acts as a surfactant and allergen. The study utilizes protein nuclear magnetic resonance spectroscopy to understand the protein’s conformation, revealing its potential role in activities such as evaporative cooling, digestion, and microbial disruption.

About Latherin

  • Latherin is a highly active surface protein found in the sweat and saliva of horses and other equid species.
  • The protein retains its surfactant properties in its native form, functioning independently of lipids or glycosylation.
  • Latherin potentially serves a variety of roles, including as a wetting agent in evaporative cooling in horses, aiding in the mastication of fibrous food, and inhibiting microbial biofilms.
  • It is part of the PLUNC family of proteins, which are abundant in the oral cavity and saliva of mammals. One other member of this protein family has also been demonstrated to function as a surfactant and capable of disrupting microbial biofilms.

Investigating the Structure of Latherin

  • The understanding of how these proteins function as surfactants while remaining soluble and compatible with cell membranes was previously unknown because their structures had not been reported.
  • The researchers utilized protein nuclear magnetic resonance spectroscopy to determine latherin’s conformation and dynamics in an aqueous solution.
  • The protein was found to exist as a monomer in the solution, possessing a slightly curved cylindrical structure with a ‘super-roll’ motif comprised of a four-stranded anti-parallel β-sheet and two opposite α-helices, which twist along the length of the cylinder.

Suggested Mechanism for Surfactant Activity

  • The molecule’s one end has noticeable, flexible loops that contain several nonpolar amino acid side chains.
  • Combining the current findings with previous biophysical observations, the researchers propose a plausible mechanism for latherin’s surfactant activity: the molecule initially localizes to the non-polar interface via the loops, then unfurls and flattens, exposing its hydrophobic interior to air or a non-polar surface.
  • Surface-active proteins are relatively rare in nature, and this is the first reported structure of such a protein in mammals.
  • Latherin’s conformation and the proposed method of action set it apart from other, non-mammalian surfactant proteins studied to date.

Cite This Article

APA
Vance SJ, McDonald RE, Cooper A, Smith BO, Kennedy MW. (2013). The structure of latherin, a surfactant allergen protein from horse sweat and saliva. J R Soc Interface, 10(85), 20130453. https://doi.org/10.1098/rsif.2013.0453

Publication

Journal of the Royal Society, Interface
ISSN: 1742-5662
NlmUniqueID: 101217269
Country: England
Language: English
Volume: 10
Issue: 85
Pages: 20130453
PII: 20130453

Researcher Affiliations

Vance, Steven J
  • School of Chemistry, University of Glasgow, Glasgow G12 8QQ, UK.
McDonald, Rhona E
    Cooper, Alan
      Smith, Brian O
        Kennedy, Malcolm W

          MeSH Terms

          • Allergens / chemistry
          • Animals
          • Fatty Acid-Binding Proteins
          • Horses
          • Models, Molecular
          • Protein Structure, Secondary
          • Protein Structure, Tertiary
          • Proteins / chemistry
          • Saliva / chemistry
          • Salivary Proteins and Peptides / chemistry
          • Structure-Activity Relationship
          • Surface-Active Agents / chemistry
          • Sweat / chemistry

          Grant Funding

          • GR070994MA / Wellcome Trust
          • Biotechnology and Biological Sciences Research Council

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