Plant lipid transfer proteins

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Plant lipid transfer protein/seed storage/trypsin-alpha amylase inhibitor
Symbol LTP/seed_store/tryp_amyl_inhib
Pfam PF00234
InterPro IPR003612

Plant lipid transfer proteins, also known as plant LTPs or PLTPs, are a group of highly-conserved proteins of about 9kDa found in higher plant tissues.[1] As its name implies, lipid transfer proteins are responsible for the shuttling of phospholipids and other fatty acid groups between cell membranes.[2] LTPs are also able to bind acyl groups.[2]

Other related proteins[edit]

Plant lipid transfer proteins share the same structural domain[3] with seed storage proteins[4] and trypsin-alpha amylase inhibitors.[5][6] The domain forms a four-helical bundle in a right-handed superhelix with a folded leaf topology, which is stabilised by disulfide bonds, and which has 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[edit]

PLTPs are pan-allergens, [7] [8] 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. [9]

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

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.[10]

Role in plant biology[edit]

These proteins in plants may be involved in:

  • cutin biosynthesis
  • surface wax formation
  • pathogen defense reactions
  • for adaptation of plants to environmental changes[11]

See also[edit]


  1. ^
  2. ^ a b
  3. ^ 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): –. doi:10.1021/bi047608v. PMID 15823028. 
  4. ^ 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): –. doi:10.1021/bi0352217. PMID 14636051. 
  5. ^ 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): –. doi:10.1021/bi971307m. PMID 9354618. 
  6. ^ 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: –. doi:10.1107/s0907444999016601. PMID 10713515. 
  7. ^
  8. ^
  9. ^ Peach allergy, M.Besler et al.
  10. ^
  11. ^ "Science Direct".