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Plant lipid transfer proteins

February 15, 2024

Plant lipid transfer proteins, also known as plant LTPs or PLTPs, are a group of highly-conserved proteins of about 7-9kDa found in higher plant tissues.[1][2] As its name implies, lipid transfer proteins facilitate the shuttling of phospholipids and other fatty acid groups between cell membranes.[3] LTPs are divided into two structurally related subfamilies according to their molecular masses: LTP1s (9 kDa) and LTP2s (7 kDa).[4] Various LTPs bind a wide range of ligands, including fatty acids with a C10–C18 chain length, acyl derivatives of coenzyme A, phospho- and galactolipids, prostaglandin B2, sterols, molecules of organic solvents, and some drugs.[2]

Plant lipid transfer protein / bifunctional inhibitor / seed storage protein, 4-helical domain
Oryza sativa Lipid Transfer Protein 1 bound to palmitic acid (black). Positive charge in blue; negative charge in red (PDB: 1UVB​).
Identifiers
SymbolLTP/seed_store/tryp_amyl_inhib
PfamPF00234
Pfam clanCL0482
InterProIPR016140
SMARTSM00499
CATH1UVB
SCOP21UVB / SCOPe / SUPFAM
CDDcd00010
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDBPDB: 1UVB​ PDB: 1afh​ PDB: 1b1u​ PDB: 1be2​ PDB: 1bea​ PDB: 1bfa​ PDB: 1bip​ PDB: 1bwo​ PDB: 1cz2​ PDB: 1fk0​ PDB: 1fk1​
Also Pfam PF13016, PF14368; see the Pfam clan relationships.

The LTP domain is also found in seed storage proteins (including 2S albumin, gliadin, and glutelin) and bifunctional trypsin/alpha-amylase inhibitors.[5][6][7][8] These proteins share the same superhelical, disulfide-stabilised four-helix bundle containing an internal cavity.

There is no sequence similarity between animal and plant LTPs. In animals, cholesteryl ester transfer protein, also called plasma lipid transfer protein, is a plasma protein that facilitates the transport of cholesteryl esters and triglycerides between the lipoproteins.

Function edit

Ordinarily, most lipids do not spontaneously exit membranes because their hydrophobicity makes them poorly soluble in water. LTPs facilitate the movement of lipids between membranes by binding, and solubilising them. LTPs typically have broad substrate specificity and so can interact with a variety of different lipids.[9]

LTPs are known to be pathogenesis-related proteins, i.e. proteins produced for pathogen defense by plants. Some LTPs are known to be antibacterial, antifungal, antiviral, and/or in vitro antiproliferative.[2] The enzyme inhibitor members are thought to regulate the development and germination of seeds as well as protect against insects and herbivores.[2]

LTPs in plants may be involved in:

Structure edit

 
Structure of OsLTP1 (white) bound to palmitic acid (black). Disulfide bridges indicated in yellow.
 
Surface charge distribution. Positive charge in blue; negative charge in red.
 
Cut-through showing internal charge distribution. Positive charge in blue; negative charge in red.
Oryza sativa Lipid Transfer Protein 1 bound to palmitic acid. (PDB: 1UVB​)

Plant lipid transfer proteins consist of 4 alpha-helices in a right-handed superhelix with a folded leaf topology. The structure is stabilised by disulfide bridges linking the helices to each other.

The structure forms an internal hydrophobic cavity in which 1-2 lipids can be bound. The outer surface of the protein is hydrophilic, allowing the complex to be soluble. The use of hydrophobic interactions, with very few charged interactions, allows the protein to have broad specificity for a range of lipids.[9]

Role in human health edit

PLTPs are pan-allergens,[11][12] and may be directly responsible for cases of food allergy. Pru p 3, the major allergen from peach, is a 9-kDa allergen belonging to the family of lipid-transfer proteins.[13] Allergic properties are closely linked with high thermal stability and resistance to gastrointestinal proteolysis of the proteins.[14] They are class 1 (gastrointestinal) food allergens that cause a more systemic response than class 2 (respiratory) allergens.[4]

Plant LTPs are considered antioxidants in a small subset of researches.[15] Whether this has value for human health is unknown.

Commercial importance edit

Lipid transfer protein 1 (from barley) is responsible, when denatured by the mashing process, for the bulk of foam which forms on top of beer.[16]

References edit

  1. ^ Asero R, Mistrello G, Roncarolo D, de Vries SC, Gautier MF, Ciurana CL, Verbeek E, Mohammadi T, Knul-Brettlova V, Akkerdaas JH, Bulder I, Aalberse RC, van Ree R (2001). "Lipid transfer protein: a pan-allergen in plant-derived foods that is highly resistant to pepsin digestion". International Archives of Allergy and Immunology. 124 (1–3): 67–9. doi:10.1159/000053671. PMID 11306929. S2CID 40934840.
  2. ^ a b c d e Finkina EI, Melnikova DN, Bogdanov IV, Ovchinnikova TV (2016). "Lipid Transfer Proteins As Components of the Plant Innate Immune System: Structure, Functions, and Applications". Acta Naturae. 8 (2): 47–61. doi:10.32607/20758251-2016-8-2-47-61. PMC 4947988. PMID 27437139.
  3. ^ Kader JC (June 1996). "Lipid-Transfer Protein in Plants". Annual Review of Plant Physiology and Plant Molecular Biology. 47: 627–654. doi:10.1146/annurev.arplant.47.1.627. PMID 15012303.
  4. ^ a b Finkina EI, Melnikova DN, Bogdanov IV, Ovchinnikova TV (2017-07-04). "Plant Pathogenesis-Related Proteins PR-10 and PR-14 as Components of Innate Immunity System and Ubiquitous Allergens". Current Medicinal Chemistry. 24 (17): 1772–1787. doi:10.2174/0929867323666161026154111. PMID 27784212.
  5. ^ Lin KF, Liu YN, Hsu ST, Samuel D, Cheng CS, Bonvin AM, Lyu PC (April 2005). "Characterization and structural analyses of nonspecific lipid transfer protein 1 from mung bean". Biochemistry. 44 (15): 5703–12. doi:10.1021/bi047608v. hdl:1874/385163. PMID 15823028.
  6. ^ Pantoja-Uceda D, Bruix M, Giménez-Gallego G, Rico M, Santoro J (December 2003). "Solution structure of RicC3, a 2S albumin storage protein from Ricinus communis". Biochemistry. 42 (47): 13839–47. doi:10.1021/bi0352217. PMID 14636051.
  7. ^ Oda Y, Matsunaga T, Fukuyama K, Miyazaki T, Morimoto T (November 1997). "Tertiary and quaternary structures of 0.19 alpha-amylase inhibitor from wheat kernel determined by X-ray analysis at 2.06 A resolution". Biochemistry. 36 (44): 13503–11. doi:10.1021/bi971307m. PMID 9354618.
  8. ^ Gourinath S, Alam N, Srinivasan A, Betzel C, Singh TP (March 2000). "Structure of the bifunctional inhibitor of trypsin and alpha-amylase from ragi seeds at 2.2 A resolution". Acta Crystallographica D. 56 (Pt 3): 287–93. doi:10.1107/s0907444999016601. PMID 10713515.
  9. ^ a b Cheng HC, Cheng PT, Peng P, Lyu PC, Sun YJ (September 2004). "Lipid binding in rice nonspecific lipid transfer protein-1 complexes from Oryza sativa". Protein Science. 13 (9): 2304–15. doi:10.1110/ps.04799704. PMC 2280015. PMID 15295114.
  10. ^ Kader, Jean-Claude (February 1997). "Lipid-transfer proteins: A puzzling family of plant proteins". Trends in Plant Science. 2 (2): 66–70. doi:10.1016/S1360-1385(97)82565-4.
  11. ^ Morris A. "Food Allergy in Detail". Surrey Allergy Clinic.
  12. ^ InterPro: IPR000528
  13. ^ Besler M, Herranz JC, Fernández-Rivas M (2000). "Peach allergy". Internet Symposium on Food Allergens. 2 (4): 185–201.
  14. ^ Bogdanov IV, Shenkarev ZO, Finkina EI, Melnikova DN, Rumynskiy EI, Arseniev AS, Ovchinnikova TV (April 2016). "A novel lipid transfer protein from the pea Pisum sativum: isolation, recombinant expression, solution structure, antifungal activity, lipid binding, and allergenic properties". BMC Plant Biology. 16: 107. doi:10.1186/s12870-016-0792-6. PMC 4852415. PMID 27137920.
  15. ^ Halliwell B (1996). "Antioxidants in human health and disease". Annual Review of Nutrition. 16: 33–50. doi:10.1146/annurev.nu.16.070196.000341. PMID 8839918.
  16. ^ . Carlsberg Research Laboratory. Archived from the original on 2016-03-03. Retrieved 2009-03-05.

February 15, 2024
plant, lipid, transfer, proteins, also, known, plant, ltps, pltps, group, highly, conserved, proteins, about, 9kda, found, higher, plant, tissues, name, implies, lipid, transfer, proteins, facilitate, shuttling, phospholipids, other, fatty, acid, groups, betwe. Plant lipid transfer proteins also known as plant LTPs or PLTPs are a group of highly conserved proteins of about 7 9kDa found in higher plant tissues 1 2 As its name implies lipid transfer proteins facilitate the shuttling of phospholipids and other fatty acid groups between cell membranes 3 LTPs are divided into two structurally related subfamilies according to their molecular masses LTP1s 9 kDa and LTP2s 7 kDa 4 Various LTPs bind a wide range of ligands including fatty acids with a C10 C18 chain length acyl derivatives of coenzyme A phospho and galactolipids prostaglandin B2 sterols molecules of organic solvents and some drugs 2 Plant lipid transfer protein bifunctional inhibitor seed storage protein 4 helical domainOryza sativa Lipid Transfer Protein 1 bound to palmitic acid black Positive charge in blue negative charge in red PDB 1UVB IdentifiersSymbolLTP seed store tryp amyl inhibPfamPF00234Pfam clanCL0482InterProIPR016140SMARTSM00499CATH1UVBSCOP21UVB SCOPe SUPFAMCDDcd00010Available protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summaryPDBPDB 1UVB PDB 1afh PDB 1b1u PDB 1be2 PDB 1bea PDB 1bfa PDB 1bip PDB 1bwo PDB 1cz2 PDB 1fk0 PDB 1fk1 Also Pfam PF13016 PF14368 see the Pfam clan relationships The LTP domain is also found in seed storage proteins including 2S albumin gliadin and glutelin and bifunctional trypsin alpha amylase inhibitors 5 6 7 8 These proteins share the same superhelical disulfide stabilised four helix bundle containing an internal cavity There is no sequence similarity between animal and plant LTPs In animals cholesteryl ester transfer protein also called plasma lipid transfer protein is a plasma protein that facilitates the transport of cholesteryl esters and triglycerides between the lipoproteins Contents 1 Function 2 Structure 3 Role in human health 4 Commercial importance 5 ReferencesFunction editOrdinarily most lipids do not spontaneously exit membranes because their hydrophobicity makes them poorly soluble in water LTPs facilitate the movement of lipids between membranes by binding and solubilising them LTPs typically have broad substrate specificity and so can interact with a variety of different lipids 9 LTPs are known to be pathogenesis related proteins i e proteins produced for pathogen defense by plants Some LTPs are known to be antibacterial antifungal antiviral and or in vitro antiproliferative 2 The enzyme inhibitor members are thought to regulate the development and germination of seeds as well as protect against insects and herbivores 2 LTPs in plants may be involved in cutin biosynthesis surface wax formation mitochondrial growth adaptation to environmental changes 10 lipid metabolism fertilization of flowering plants adaptation of plants under stress conditions activation and regulation of signaling cascades apoptosis symbiosis fruit ripening 2 Structure edit nbsp Structure of OsLTP1 white bound to palmitic acid black Disulfide bridges indicated in yellow nbsp Surface charge distribution Positive charge in blue negative charge in red nbsp Cut through showing internal charge distribution Positive charge in blue negative charge in red Oryza sativa Lipid Transfer Protein 1 bound to palmitic acid PDB 1UVB Plant lipid transfer proteins consist of 4 alpha helices in a right handed superhelix with a folded leaf topology The structure is stabilised by disulfide bridges linking the helices to each other The structure forms an internal hydrophobic cavity in which 1 2 lipids can be bound The outer surface of the protein is hydrophilic allowing the complex to be soluble The use of hydrophobic interactions with very few charged interactions allows the protein to have broad specificity for a range of lipids 9 Role in human health editPLTPs are pan allergens 11 12 and may be directly responsible for cases of food allergy Pru p 3 the major allergen from peach is a 9 kDa allergen belonging to the family of lipid transfer proteins 13 Allergic properties are closely linked with high thermal stability and resistance to gastrointestinal proteolysis of the proteins 14 They are class 1 gastrointestinal food allergens that cause a more systemic response than class 2 respiratory allergens 4 Plant LTPs are considered antioxidants in a small subset of researches 15 Whether this has value for human health is unknown Commercial importance editLipid transfer protein 1 from barley is responsible when denatured by the mashing process for the bulk of foam which forms on top of beer 16 References edit Asero R Mistrello G Roncarolo D de Vries SC Gautier MF Ciurana CL Verbeek E Mohammadi T Knul Brettlova V Akkerdaas JH Bulder I Aalberse RC van Ree R 2001 Lipid transfer protein a pan allergen in plant derived foods that is highly resistant to pepsin digestion International Archives of Allergy and Immunology 124 1 3 67 9 doi 10 1159 000053671 PMID 11306929 S2CID 40934840 a b c d e Finkina EI Melnikova DN Bogdanov IV Ovchinnikova TV 2016 Lipid Transfer Proteins As Components of the Plant Innate Immune System Structure Functions and Applications Acta Naturae 8 2 47 61 doi 10 32607 20758251 2016 8 2 47 61 PMC 4947988 PMID 27437139 Kader JC June 1996 Lipid Transfer Protein in Plants Annual Review of Plant Physiology and Plant Molecular Biology 47 627 654 doi 10 1146 annurev arplant 47 1 627 PMID 15012303 a b Finkina EI Melnikova DN Bogdanov IV Ovchinnikova TV 2017 07 04 Plant Pathogenesis Related Proteins PR 10 and PR 14 as Components of Innate Immunity System and Ubiquitous Allergens Current Medicinal Chemistry 24 17 1772 1787 doi 10 2174 0929867323666161026154111 PMID 27784212 Lin KF Liu YN Hsu ST Samuel D Cheng CS Bonvin AM Lyu PC April 2005 Characterization and structural analyses of nonspecific lipid transfer protein 1 from mung bean Biochemistry 44 15 5703 12 doi 10 1021 bi047608v hdl 1874 385163 PMID 15823028 Pantoja Uceda D Bruix M Gimenez Gallego G Rico M Santoro J December 2003 Solution structure of RicC3 a 2S albumin storage protein from Ricinus communis Biochemistry 42 47 13839 47 doi 10 1021 bi0352217 PMID 14636051 Oda Y Matsunaga T Fukuyama K Miyazaki T Morimoto T November 1997 Tertiary and quaternary structures of 0 19 alpha amylase inhibitor from wheat kernel determined by X ray analysis at 2 06 A resolution Biochemistry 36 44 13503 11 doi 10 1021 bi971307m PMID 9354618 Gourinath S Alam N Srinivasan A Betzel C Singh TP March 2000 Structure of the bifunctional inhibitor of trypsin and alpha amylase from ragi seeds at 2 2 A resolution Acta Crystallographica D 56 Pt 3 287 93 doi 10 1107 s0907444999016601 PMID 10713515 a b Cheng HC Cheng PT Peng P Lyu PC Sun YJ September 2004 Lipid binding in rice nonspecific lipid transfer protein 1 complexes from Oryza sativa Protein Science 13 9 2304 15 doi 10 1110 ps 04799704 PMC 2280015 PMID 15295114 Kader Jean Claude February 1997 Lipid transfer proteins A puzzling family of plant proteins Trends in Plant Science 2 2 66 70 doi 10 1016 S1360 1385 97 82565 4 Morris A Food Allergy in Detail Surrey Allergy Clinic InterPro IPR000528 Besler M Herranz JC Fernandez Rivas M 2000 Peach allergy Internet Symposium on Food Allergens 2 4 185 201 Bogdanov IV Shenkarev ZO Finkina EI Melnikova DN Rumynskiy EI Arseniev AS Ovchinnikova TV April 2016 A novel lipid transfer protein from the pea Pisum sativum isolation recombinant expression solution structure antifungal activity lipid binding and allergenic properties BMC Plant Biology 16 107 doi 10 1186 s12870 016 0792 6 PMC 4852415 PMID 27137920 Halliwell B 1996 Antioxidants in human health and disease Annual Review of Nutrition 16 33 50 doi 10 1146 annurev nu 16 070196 000341 PMID 8839918 Foam Carlsberg Research Laboratory Archived from the original on 2016 03 03 Retrieved 2009 03 05 Retrieved from https en wikipedia org w index php title Plant lipid transfer proteins amp oldid 1188100433, wikipedia, wiki, book, books, library,

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