Plant lipid transfer proteins: Difference between revisions

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remove seed storage / trypsin-alpha amylase inhibitor from infobox. Discussed later in article.
I made the description of the proteins broader, however it is still extremely poor, because there is a lot information about these proteins. I added some information into general description, Function topic, Role in human health topic, created Biological activity topic.
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{{Pfam box |Symbol = LTP/seed_store/tryp_amyl_inhib |Name = Plant lipid transfer protein |image = File:Surface_1UVB.png |caption = [[Oryza sativa]] Lipid Transfer Protein 1 bound to [[Palmitic acid]] (black). Positive charge in blue, negative charge in red. (PDB:1UVB [http://www.rcsb.org/pdb/explore/explore.do?structureId=1uvb]) |Pfam = PF00234 |InterPro = IPR003612 |SMART = SM00499 |SCOP = |PDB = {{PDB|1UVB}} {{PDB|1afh}} {{PDB|1b1u}} {{PDB|1be2}} {{PDB|1bea}} {{PDB|1bfa}} {{PDB|1bip}} {{PDB|1bwo}} {{PDB|1cz2}} {{PDB|1fk0}} {{PDB|1fk1}} }}
{{Pfam box |Symbol = LTP/seed_store/tryp_amyl_inhib |Name = Plant lipid transfer protein |image = File:Surface_1UVB.png |caption = [[Oryza sativa]] Lipid Transfer Protein 1 bound to [[Palmitic acid]] (black). Positive charge in blue, negative charge in red. (PDB:1UVB [http://www.rcsb.org/pdb/explore/explore.do?structureId=1uvb]) |Pfam = PF00234 |InterPro = IPR003612 |SMART = SM00499 |SCOP = |PDB = {{PDB|1UVB}} {{PDB|1afh}} {{PDB|1b1u}} {{PDB|1be2}} {{PDB|1bea}} {{PDB|1bfa}} {{PDB|1bip}} {{PDB|1bwo}} {{PDB|1cz2}} {{PDB|1fk0}} {{PDB|1fk1}} }}


'''Plant lipid transfer proteins''', also known as plant '''LTP'''s or PLTPs, are a group of highly-[[conserved sequence|conserved]] [[protein]]s of about 9[[kDa]] found in [[vascular plant|higher plant]] tissues.<ref>http://content.karger.com/ProdukteDB/produkte.asp?Doi=53671</ref> As its name implies, lipid transfer proteins are responsible for the [[molecular shuttle|shuttling]] of [[phospholipid]]s and other [[fatty acid]] groups between [[cell membrane]]s.<ref name="arjournals.annualreviews.org">http://arjournals.annualreviews.org/doi/abs/10.1146/annurev.arplant.47.1.627?cookieSet=1&journalCode=arplant.2</ref> LTPs are also able to bind [[acyl]] groups.<ref name="arjournals.annualreviews.org"/>
'''Plant lipid transfer proteins''', also known as plant '''LTP'''s or PLTPs, are a group of highly-[[conserved sequence|conserved]] [[protein]]s of about 7-9[[kDa]] found in [[vascular plant|higher plant]] tissues.<ref>http://content.karger.com/ProdukteDB/produkte.asp?Doi=53671</ref><ref name=":0">{{Cite journal|last=Finkina|first=E. I.|last2=Melnikova|first2=D. N.|last3=Bogdanov|first3=I. V.|last4=Ovchinnikova|first4=T. V.|date=2016|title=Lipid Transfer Proteins As Components of the Plant Innate Immune System: Structure, Functions, and Applications|url=https://www.ncbi.nlm.nih.gov/pubmed/27437139|journal=Acta Naturae|volume=8|issue=2|pages=47–61|issn=2075-8251|pmc=PMC4947988|pmid=27437139|via=}}</ref> As its name implies, lipid transfer proteins are responsible for the [[molecular shuttle|shuttling]] of [[phospholipid]]s and other [[fatty acid]] groups between [[cell membrane]]s.<ref name="arjournals.annualreviews.org">http://arjournals.annualreviews.org/doi/abs/10.1146/annurev.arplant.47.1.627?cookieSet=1&journalCode=arplant.2</ref> LTPs are divided into two structurallyrelated subfamilies according to their molecular masses: LTP1s (9 kDa) and LTP2s (7 kDa).<ref name=":1">{{Cite journal|last=Finkina|first=Ekaterina I.|last2=Melnikova|first2=Daria N.|last3=Bogdanov|first3=Ivan V.|last4=Ovchinnikova|first4=Tatiana V.|date=2017-07-04|title=Plant Pathogenesis-Related Proteins PR-10 and PR-14 as Components of Innate Immunity System and Ubiquitous Allergens|url=http://www.eurekaselect.com/146732/article|journal=Current Medicinal Chemistry|language=en|volume=24|issue=17|doi=10.2174/0929867323666161026154111|issn=0929-8673}}</ref> Various LTPs bind a wide range of ligands, including fatty acids (FAs) with a C<sub>10</sub>–C<sub>18</sub> chain length, acyl derivatives of coenzyme A (CoA), phospho- and galactolipids, prostaglandin B<sub>2</sub>, sterols, molecules of organic solvents, and some drugs.<ref name=":0" /> LTP2

== Biological activity ==
LTPs constitute one of the classes of defense PRPs, many of which have antimicrobial and enzymatic activities or are enzyme inhibitors. Different proteins of this class can exhibit the following activities:<ref name=":0" />

* antibacterial
* antifungal
* antiviral
* antiproliferative

and inhibit some enzymes.


==Function==
==Function==
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*pathogen defense reactions
*pathogen defense reactions
*adaptation to environmental changes<ref>{{cite journal|title=Science Direct|url=http://www.sciencedirect.com/science/article/pii/S1360138597825654 | doi=10.1016/S1360-1385(97)82565-4 | volume=2|journal=Trends in Plant Science|pages=66–70}}</ref>
*adaptation to environmental changes<ref>{{cite journal|title=Science Direct|url=http://www.sciencedirect.com/science/article/pii/S1360138597825654 | doi=10.1016/S1360-1385(97)82565-4 | volume=2|journal=Trends in Plant Science|pages=66–70}}</ref>
*lipid metabolism
*fertilization of flowering plants
*adaptation of plants under stress conditions
*activation and regulation of signaling cascades
*apoptosis
*symbiosis
*fruit ripening<ref name=":0" />


==Structure==
==Structure==
Line 49: Line 66:
and may be directly responsible for cases of [[food allergy]].
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.
Pru p 3, the major [[allergen]] from [[peach]], is a 9-kDa allergen belonging to the family of lipid-transfer proteins.
<ref>http://www.food-allergens.de/symposium-2-4/peach/peach-allergens.htm Peach allergy, M.Besler et al.</ref> Allergic properties are closely linked with high thermal stability and resistance to gastrointestinal proteolysis of the proteins.<ref>{{Cite journal|last=Bogdanov|first=Ivan V.|last2=Shenkarev|first2=Zakhar O.|last3=Finkina|first3=Ekaterina I.|last4=Melnikova|first4=Daria N.|last5=Rumynskiy|first5=Eugene I.|last6=Arseniev|first6=Alexander S.|last7=Ovchinnikova|first7=Tatiana V.|date=2016-04-30|title=A novel lipid transfer protein from the pea Pisum sativum: isolation, recombinant expression, solution structure, antifungal activity, lipid binding, and allergenic properties|url=https://doi.org/10.1186/s12870-016-0792-6|journal=BMC Plant Biology|volume=16|pages=107|doi=10.1186/s12870-016-0792-6|issn=1471-2229|pmc=PMC4852415|pmid=27137920}}</ref> Many of the LTP allergens are able to cause not only manifestation of allergic reactions but also sensitization via the gastrointestinal tract, beeng thus class I food allergens.<ref name=":1" /> In contrast, class II food allergens are able only to elicit allergic symptoms due to its cross-reactivity with major sensitizer.
<ref>http://www.food-allergens.de/symposium-2-4/peach/peach-allergens.htm Peach allergy, M.Besler et al.</ref>

*[http://www.annualreviews.org/doi/abs/10.1146/annurev.nu.16.070196.000341?journalCode=nutr]
*[http://www.annualreviews.org/doi/abs/10.1146/annurev.nu.16.070196.000341?journalCode=nutr]
They are used as antioxidants and prevent diseases.{{citation needed|date=September 2014}}
They are used as antioxidants and prevent diseases.{{citation needed|date=September 2014}}

Revision as of 15:05, 29 May 2018

Plant lipid transfer protein
Oryza sativa Lipid Transfer Protein 1 bound to Palmitic acid (black). Positive charge in blue, negative charge in red. (PDB:1UVB [1])
Identifiers
SymbolLTP/seed_store/tryp_amyl_inhib
PfamPF00234
InterProIPR003612
SMARTSM00499
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​

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 are responsible for the shuttling of phospholipids and other fatty acid groups between cell membranes.[3] LTPs are divided into two structurallyrelated 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 (FAs) with a C10–C18 chain length, acyl derivatives of coenzyme A (CoA), phospho- and galactolipids, prostaglandin B2, sterols, molecules of organic solvents, and some drugs.[2] LTP2

Biological activity

LTPs constitute one of the classes of defense PRPs, many of which have antimicrobial and enzymatic activities or are enzyme inhibitors. Different proteins of this class can exhibit the following activities:[2]

  • antibacterial
  • antifungal
  • antiviral
  • antiproliferative

and inhibit some enzymes.

Function

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.[5]

LTPs in plants may be involved in:

  • cutin biosynthesis
  • surface wax formation
  • mitochondrial growth
  • pathogen defense reactions
  • adaptation to environmental changes[6]
  • lipid metabolism
  • fertilization of flowering plants
  • adaptation of plants under stress conditions
  • activation and regulation of signaling cascades
  • apoptosis
  • symbiosis
  • fruit ripening[2]

Structure

Structure of OsLTP1 (white) bound to Palmitic acid (black). Disulphides 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 bonds 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.[5]

Other related proteins

Plant lipid transfer proteins share the same structural domain[7] with seed storage proteins[8] and trypsin-alpha amylase inhibitors.[9][10] These proteins share the same superhelical, disulphide-stabilised four-helix bundle containing an internal cavity.

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

Role in human health

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] Many of the LTP allergens are able to cause not only manifestation of allergic reactions but also sensitization via the gastrointestinal tract, beeng thus class I food allergens.[4] In contrast, class II food allergens are able only to elicit allergic symptoms due to its cross-reactivity with major sensitizer.

They are used as antioxidants and prevent diseases.[citation needed]

Commercial importance

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.[15]

See also

References

  1. ^ http://content.karger.com/ProdukteDB/produkte.asp?Doi=53671
  2. ^ a b c d Finkina, E. I.; Melnikova, D. N.; Bogdanov, I. V.; Ovchinnikova, T. V. (2016). "Lipid Transfer Proteins As Components of the Plant Innate Immune System: Structure, Functions, and Applications". Acta Naturae. 8 (2): 47–61. ISSN 2075-8251. PMC 4947988. PMID 27437139.{{cite journal}}: CS1 maint: PMC format (link)
  3. ^ http://arjournals.annualreviews.org/doi/abs/10.1146/annurev.arplant.47.1.627?cookieSet=1&journalCode=arplant.2
  4. ^ a b Finkina, Ekaterina I.; Melnikova, Daria N.; Bogdanov, Ivan V.; Ovchinnikova, Tatiana V. (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). doi:10.2174/0929867323666161026154111. ISSN 0929-8673.
  5. ^ 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.
  6. ^ "Science Direct". Trends in Plant Science. 2: 66–70. doi:10.1016/S1360-1385(97)82565-4.
  7. ^ Bonvin AM, Lyu PC, Samuel D, Cheng CS, Lin KF, Liu YN, Hsu ST (2005). "Characterization and structural analyses of nonspecific lipid transfer protein 1 from mung bean". Biochemistry. 44 (15): 5703–12. doi:10.1021/bi047608v. PMID 15823028.
  8. ^ Bruix M, Santoro J, Rico M, Gimenez-Gallego G, Pantoja-Uceda D (2003). "Solution structure of RicC3, a 2S albumin storage protein from Ricinus communis". Biochemistry. 42 (47): 13839–47. doi:10.1021/bi0352217. PMID 14636051.
  9. ^ Fukuyama K, Oda Y, Morimoto T, Matsunaga T, Miyazaki T (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.
  10. ^ Betzel C, Srinivasan A, Singh TP, Gourinath S, Alam N (2000). "Structure of the bifunctional inhibitor of trypsin and alpha-amylase from ragi seeds at 2.2 A resolution". Acta Crystallogr. D. 56 (Pt 3): 287–93. doi:10.1107/s0907444999016601. PMID 10713515.
  11. ^ http://www.allergy-clinic.co.uk/food-allergy/food-allergy-guide/
  12. ^ http://www.ebi.ac.uk/interpro/IEntry?ac=IPR000528
  13. ^ http://www.food-allergens.de/symposium-2-4/peach/peach-allergens.htm Peach allergy, M.Besler et al.
  14. ^ Bogdanov, Ivan V.; Shenkarev, Zakhar O.; Finkina, Ekaterina I.; Melnikova, Daria N.; Rumynskiy, Eugene I.; Arseniev, Alexander S.; Ovchinnikova, Tatiana V. (2016-04-30). "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. ISSN 1471-2229. PMC 4852415. PMID 27137920.{{cite journal}}: CS1 maint: PMC format (link) CS1 maint: unflagged free DOI (link)
  15. ^ http://www.crc.dk/flab/foam.htm
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