PFAM PF00234; tryp_alpha_amyl; non specific lipid transfer subfamily.
Sequence Known?:
No
Allergen accession No.s:
Not determined
3D Structure Accession No.:
Not determined
Calculated Masses:
Not determined
Experimental Masses:
10 kDa
Oligomeric Masses:
Monomeric
Allergen epitopes:
Not known
Allergen stability: Process, chemical, enzymatic
Not known but many ns-LTPs are stable proteins, which tend to be resistant to denaturation and proteolysis.
Nature of main cross-reacting proteins:
ns-LTPs from Rosaceae fruits and other plants show IgE cross-reactivity.
Allergen properties & biological function:
ns-LTPs bind and transfer lipids in vitro but their in vivo role in plants is not clear. They have a protective function and form the PR14 family of pathogenesis response proteins. They may be involved in the transport of suberin in the formation of cutin.
Allergen purification:
Not described.
Other biochemical information:
The IgE reactivity of sera to walnut extract could be 74-100% inhibited by peach ns-LTP in 11 walnut allergic patients (Asero et al. 2002 [667]).
References (1)
Asero R, Mistrello G, Roncarolo D, Amato S, Caldironi G, Barocci F, van Ree R.
Immunological cross-reactivity between lipid transfer proteins from botanically unrelated plant-derived foods: a clinical study.
Allergy 57(10):900-906 2002
PUBMED ID:
12269935
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