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Home / Equine Research Bank / Biomol NMR Assign / Resonance assignments for latherin, a natural surfactant pro...
Biomolecular NMR assignments2013; 8(1); 213-216; doi: 10.1007/s12104-013-9485-3

Resonance assignments for latherin, a natural surfactant protein from horse sweat.

Abstract: Latherin is an intrinsically surfactant protein of ~23 kDa found in the sweat and saliva of horses. Its function is probably to enhance the translocation of sweat water from the skin to the surface of the pelt for evaporative cooling. Its role in saliva may be to enhance the wetting, softening and maceration of the dry, fibrous food for which equines are adapted. Latherin is unusual in its relatively high content of aliphatic amino acids (~25% leucines) that might contribute to its surfactant properties. Latherin is related to the palate, lung, and nasal epithelium carcinoma-associated proteins (PLUNCs) of mammals, at least one of which is now known to exhibit similar surfactant activity to latherin. No structures of any PLUNC protein are currently available. (15)N,(13)C-labelled recombinant latherin was produced in Escherichia coli, and essentially all of the resonances were assigned despite the signal overlap due to the preponderance of leucines. The most notable exceptions include a number of residues located in an apparently dynamic loop region between residues 145 and 154. The assignments have been deposited with BMRB accession number 19067.
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Publication Date: 2013-05-26 PubMed ID: 23708874PubMed Central: PMC3955484DOI: 10.1007/s12104-013-9485-3Google Scholar: Lookup
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  • Journal Article
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  • Non-U.S. Gov't

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.

The research article is about latherin, a surfactant protein found in horse sweat and saliva, and its properties. The researchers produced a labelled version of this protein in a bacteria strain and carried out a study to identify its structure.

Introduction

  • The article focuses on latherin, a protein found in horse sweat and saliva. This protein is a natural surfactant and possibly plays a role in moving sweat water from the skin to the hair surface for cooling purposes.
  • It may also assist in making hard, fibrous food softer and easier for horses to consume by increasing moisture in the horse’s mouth.

Characteristics of Latherin

  • Latherin stands out due to its high content of aliphatic amino acids—specifically leucines—which is speculated to contribute to its surfactant properties.
  • Latherin is similar to certain proteins found in mammals, referred to as PLUNCs (palate, lung, and nasal epithelium carcinoma-associated proteins). Some PLUNCs also show surfactant activity resembling that of latherin.
  • Unfortunately, no structures of any PLUNC protein are currently available, limiting our understanding of this family of proteins.

Research Methodology

  • The researchers produced labelled versions of latherin in E.coli—an often-used bacteria type in recombinant protein production.
  • The labelled protein enabled them to study its structure despite the signal overlap caused by the many leucines.

Findings

  • All resonances of the produced protein were assigned, with the exception of a few located in a seemingly dynamic loop region between residue numbers 145 and 154. This means they could identify most parts of the protein’s structure, except for a specific region that seemed to be changing.
  • The results were deposited with BMRB (BioMagResBank), a repository for data from NMR spectroscopy, under the accession number 19067, for further research by others in the field.

Cite This Article

APA
Vance SJ, McDonald RE, Cooper A, Kennedy MW, Smith BO. (2013). Resonance assignments for latherin, a natural surfactant protein from horse sweat. Biomol NMR Assign, 8(1), 213-216. https://doi.org/10.1007/s12104-013-9485-3

Publication

Biomolecular NMR assignments
ISSN: 1874-270X
NlmUniqueID: 101472371
Country: Netherlands
Language: English
Volume: 8
Issue: 1
Pages: 213-216

Researcher Affiliations

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

          MeSH Terms

          • Animals
          • Fatty Acid-Binding Proteins
          • Horses
          • Nuclear Magnetic Resonance, Biomolecular
          • Proteins / chemistry
          • Surface-Active Agents / chemistry
          • Sweat / metabolism

          Grant Funding

          • Wellcome Trust
          • 070994 / Wellcome Trust
          • Biotechnology and Biological Sciences Research Council

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          Citations

          This article has been cited 3 times.
          1. Muñoz-Prieto A, Escribano D, Contreras-Aguilar MD, Horvatić A, Guillemin N, Jacobsen S, Cerón JJ, Mrljak V. Tandem Mass Tag (TMT) Proteomic Analysis of Saliva in Horses with Acute Abdominal Disease. Animals (Basel) 2021 Apr 30;11(5).
            doi: 10.3390/ani11051304pubmed: 33946607google scholar: lookup
          2. Victor S, Binnmyr J, Lampa E, Rask-Andersen A, Elfman L. Levels of horse allergen Equ c 4 in dander and saliva from ten horse breeds. Clin Exp Allergy 2019 May;49(5):701-711.
            doi: 10.1111/cea.13362pubmed: 30716182google scholar: lookup
          3. Vance SJ, McDonald RE, Cooper A, Smith BO, Kennedy MW. The structure of latherin, a surfactant allergen protein from horse sweat and saliva. J R Soc Interface 2013 Aug 6;10(85):20130453.
            doi: 10.1098/rsif.2013.0453pubmed: 23782536google scholar: lookup
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