ArticleJournal of the Royal Society, Interface2013
The structure of latherin, a surfactant allergen protein from horse sweat and saliva.
Article in Journal of the Royal Society, Interface, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 60 citations in OpenAlex.
- A lipid-binding protein in black-legged tick saliva selectively recognizesbioRxiv : the preprint server for biology · 2026Article
- Sensitization to Horse Allergens-Molecular Analysis Based on the Results of Multiparameter Tests.International journal of molecular sciences · 2025Article
- Foam fractionation Tags (F-Tags) enabling surfactant-free, activity-preserving recovery of enzymes.Applied microbiology and biotechnology · 2024Article
- Tandem Mass Tag (TMT) Proteomic Analysis of Saliva in Horses with Acute Abdominal Disease.Animals : an open access journal from MDPI · 2021Article
- Equine Hypersensitivity: the Dark Horse of Allergy.Clinical reviews in allergy & immunology · 2020Review
- The parotid secretory protein BPIFA2 is a salivary surfactant that affects lipopolysaccharide action.Experimental physiology · 2020Article
- Synthesis and characterization of geminis and implications of their micellar solution on ninhydrin and metal amino acid complex.Royal Society open science · 2020Article
- Human and Nonhuman Primate Lineage-Specific Footprints in the Salivary Proteome.Molecular biology and evolution · 2020Article
- Whole genome detection of sequence and structural polymorphism in six diverse horses.PloS one · 2020Article
- Remote homology searches identify bacterial homologues of eukaryotic lipid transfer proteins, including Chorein-N domains in TamB and AsmA and Mdm31p.BMC molecular and cell biology · 2019Article
- Levels of horse allergen Equ c 4 in dander and saliva from ten horse breeds.Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology · 2019Article
- Lipophilic Allergens, Different Modes of Allergen-Lipid Interaction and Their Impact on Asthma and Allergy.Frontiers in immunology · 2019Review
- Article
- Crystal structure of the mouse innate immunity factor bacterial permeability-increasing family member A1.Acta crystallographica. Section F, Structural biology communications · 2018Article
- Frog foams and natural protein surfactants.Colloids and surfaces. A, Physicochemical and engineering aspects · 2017Article
- Tubular lipid binding proteins (TULIPs) growing everywhere.Biochimica et biophysica acta. Molecular cell research · 2017Review
- Respiratory Allergens from Furred Mammals: Environmental and Occupational Exposure.Veterinary sciences · 2017Review
- Open sesame: Identification of sesame oil and oil soot ink in organic deposits of Tang Dynasty lamps from Astana necropolis in China.PloS one · 2017Article
- The Diverse Structures and Functions of Surfactant Proteins.Trends in biochemical sciences · 2016Review
- Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
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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