clear search
Recent searches Clear History
Contact Us

k221 Hev b 8 Profilin, Latex

Allergen Component
Biological Function Actin-binding protein.
Code k221
LOINC 56597-8
Source Material rHev b 8 is a CCD-free recombinant protein
Latin Name Hevea brasiliensis
Common Name Profilin
Categories Occupational allergens
Molecular Weight 14 kDa

Molecular Aspects


Hev b 8 (13,56-58,60) is a profilin. Plant profilins are important panallergens. They are responsible for a significant percentage of pollen-related allergies. The observed frequencies of Hev b 8-specific IgE antibodies in sera of Latex-allergic patients in different risk groups range between 6 and 24% (1,57-58,60).

rHev b 8 has a sequence identity of 75% with Birch profilin (Bet v 2) (57). Recombinant isoforms of Hev b 8 with marginal differences in the amino acid sequence were reported to have no influence on the IgE-binding properties of the rHev b 8 isoforms. In a study evaluating the prevalence of serum IgE antibodies to rHev b 8, among 17 SB patients, IgE antibodies to rHev b 8 were found in 2, and in 5 of 25 sera (20%) from HCW. Further studies demonstrated the presence of IgE-binding epitopes on the Hev b 8 molecule which did not cross-react with Birch profilin. The study concluded that Latex profilin represents a minor allergen in Natural rubber latex (NRL) and may have IgE-binding epitopes different from Bet v 2 (58).

These factors may explain the variability in the prevalence of allergen-specific IgE binding to Latex profilin in studies. For example, skin tests and allergen-specific IgE antibodies to natural and recombinant purified Hev b 8 were positive in 15 of 17 spina bifida (SB) children and all 14 adults allergic to Latex. However, only 42% of the Latex-allergic patients had allergen-specific IgE levels of 0.35 kUA/L or higher, and only 39% of them exhibited IgE binding with any natural or recombinant Hev b 8 forms (56).

Between 30% and 50% of individuals who are allergic to Latex products are also allergic to specific plant foods, and this is aptly described as Latex-fruit syndrome. However, the roles of the Latex chitinase, Latex profilin and Latex beta-1,3-glucanase need to be clarified. This is well illustrated in a study, which reviewed simultaneous sensitisation to Latex and Bell pepper, sensitisation that had previously been reported. In sera of 4 patients with allergy to Latex and Bell pepper, 3 were shown to have IgE antibodies to profilin from Bell pepper and Latex. Two patients also had IgE antibodies to Hev b 2 (a beta-1,3-glucanase) and a homologous protein in Bell pepper. One patient was shown to have allergen-specific IgE to an L-ascorbate peroxidase, and another patient to a 38 kDa protein. The study concluded that Hev b 2 (beta-1,3-glucanase) and the Bell pepper L-ascorbate peroxidase were also cross-reactive allergens, and that profilin was responsible for some of the IgE cross-reactivity (59).

Similarly, other studies have demonstrated the variable responsibility of profilin in cross-reactivity between Latex profilin and other plant profilins. In a study of sera of 36 individuals containing IgE antibodies to Ragweed profilin, 35 reacted with profilin from Latex, indicating structural homologies between profilins from Latex and Ragweed. Fifty-nine percent of these sera were found to be positive for Latex-specific IgE. As profilin is also present in Banana, it was proposed that Latex profilin would likely be involved in cross-reactivity between Banana and Latex. However, among 19 individuals allergic to Latex, only 2 had anti-profilin IgE antibodies. The authors suggested that IgE antibodies to Latex profilin might be a questionable factor in sensitisation of occupationally exposed patients, but that sensitisation to profilin should be taken into account when interpreting the results of Latex-specific IgE investigation (60).

Recombinant profilin from Banana and Pineapple has a high sequence identity (71-84%) to known allergenic pollen and food profilin. In a study demonstrating IgE binding in sera to recombinant profilin, in 7/16 (44%) subjects with suspected Banana allergy, and in 8/19 (42%) subjects with suspected Pineapple allergy, high cross-reactivity to Birch pollen profilin Bet v 2 and Latex profilin Hev b 8 was demonstrated. Profilin was therefore shown to be an important mediator of IgE cross-reactivity between pollen and exotic fruits (61-62).

In a study using rHev b 8 to screen sera from Latex-allergic HCW with well-documented histories of food and pollen allergy and Latex-allergic SB patients, 12 of the 50 HCW and 2 of the 34 SB patients were sensitised to Hev b 8. All Hev b 8-sensitised patients showed allergic symptoms to pollen or plant foods. Cross-reactivity among profilins of Latex, pollen and plant food was demonstrated by their ability to inhibit IgE binding to rHev b 8. The authors concluded that primary sensitisation to Latex profilin in the majority of cases took place via pollen or food profilin, and that pollen- and food-allergic patients with profilin-specific IgE antibodies could be at risk of developing Latex allergy (57).

Other studies have also demonstrated the relevance of Latex profilin cross-reactivity, for example between Chenopodium profilin and Latex (65), and between 2 Rice profilin cDNAs (highly homologous to each other) and profilin from Maize, Bermuda grass, Timothy grass and Latex (63).

  1. Rihs H-P, Raulf-Heimsoth M. Natural rubber latex allergens: Characterization and evaluation of their allergenic capacity. New Horizons, Pharmacia Diagnostics AB 2003;No 3
  2. Yunginger JW, Jones, RT, Fransway AF, Kelso JM et al. Extractable latex allergens and proteins in disposable medical gloves and other other rubber products.
    J Allergy Clin Immunol 1994;93:836-42
  3. Sussman GL, Beezhold DH, Kurup VP. Allergens and natural rubber proteins.
    J Allergy Clin Immunol 2002;110(2 Pt 2):S033-9
  4. Posch A, Chen Z, Dunn MJ, Wheeler CH, Petersen A, Leubner-Metzger G, Baur X. Latex allergen database.
    Electrophoresis 1997;18(15):2803-10
  5. Posch A, Chen Z, Wheeler C, Dunn MJ, Raulf-Heimsoth M, Baur X. Characterization and identification of latex allergens by two-dimensional electrophoresis and protein microsequencing.
    J Allergy Clin Immunol 1997;99(3):385-95
  6. Yagami T, Haishima Y, Tsuchiya T, Tomitaka-Yagami A, Kano H, Matsunaga K. Proteomic analysis of putative latex allergens.
    Int Arch Allergy Immunol 2004;135(1):3-11
  7. Yeang HY. Natural rubber latex allergens: new developments. Curr Opin Allergy Clin Immunol 2004;4(2):99-104
  8. Salcedo G, Diaz-Perales A, Sanchez-Monge R. The role of plant panallergens in sensitization to natural rubber latex. Curr Opin Allergy Clin Immunol 2001;1(2):177-83
  9. Bernstein DI, Biagini RE, Karnani R, Hamilton R, Murphy K, Bernstein C, Arif SA, Berendts B, Yeang HY. In vivo sensitization to purified Hevea brasiliensis proteins in health care workers sensitized to natural rubber latex.
    J Allergy Clin Immunol 2003;111(3):610-6
  10. Wagner B, Buck D, Hafner C, Sowka S, Niggemann B, Scheiner O, Breiteneder H. Hev b 7 is a Hevea brasiliensis protein associated with latex allergy in children with spina bifida.
    J Allergy Clin Immunol 2001;108(4):621-7
  11. Yeang HY, Chow KS, Yusof F, Arif SA, Chew NP, Loke YH. Appraisal of latex glove proteins in the induction of sensitivity to multiple latex allergens. J Investig Allergol Clin Immunol 2000;10(4):215-22
  12. Kurup VP, Yeang HY, Sussman GL, Bansal NK, Beezhold DH, Kelly KJ, Hoffman DR, Williams B, Fink JN. Detection of immunoglobulin antibodies in the sera of patients using purified latex allergens.
    Clin Exp Allergy 2000;30(3):359-69
  13. Yip L, Hickey V, Wagner B, Liss G, Slater J, Breiteneder H, Sussman G, Beezhold D. Skin prick test reactivity to recombinant latex allergens.
    Int Arch Allergy Immunol 2000;121(4):292-9
  14. Ylitalo L, Alenius H, Turjanmaa K, Palosuo T, Reunala T. IgE antibodies to prohevein, hevein, and rubber elongation factor in children with latex allergy. J Allergy Clin Immunol 1998;102(4 Pt 1):659-64
  15. Yeang HY, Arif SA, Raulf-Heimsoth M, Loke YH, Sander I, Sulong SH, Lau CH, Hamilton RG. Hev b 5 and Hev b 13 as allergen markers to estimate the allergenic potency of latex gloves.
    J Allergy Clin Immunol 2004;114(3):593-8
  16. Banerjee B, Kanitpong K, Fink JN, Zussman M, Sussman GL, Kelly KJ, Kurup VP. Unique and shared IgE epitopes of Hev b 1 and Hev b 3 in latex allergy.
    Mol Immunol 2000;37(12-13):789-98
  17. Yeang HY, Cheong KF, Sunderasan E, Hamzah S, Chew NP, Hamid S, Hamilton RG, Cardosa MJ. The 14.6 kd rubber elongation factor (Hev b 1) and 24 kd (Hev b 3) rubber particle proteins are recognized by IgE from patients with spina bifida and latex allergy.
    J Allergy Clin Immunol 1996;98(3):628-39
  18. Rihs HP, Chen Z, Schumacher S, Rozynek P, Cremer R, Lundberg M, Raulf-Heimsoth M, Petersen A, Baur X. Recombinant Hev b 1: large-scale production and immunological characterization.
    Clin Exp Allergy 2000;30(9):1285-92
  19. Chen Z, Van Kampen V, Raulf-Heimsoth M, Baur X. Allergenic and antigenic determinants of latex allergen Hev b 1: peptide mapping of epitopes recognized by human, murine and rabbit antibodies.
    Clin Exp Allergy 1996;26(4):406-15
  20. Raulf-Heimsoth M, Chen Z, Liebers V, Allmers H, Baur X. Lymphocyte proliferation response to extracts from different latex materials and to the purified latex allergen Hev b 1 (rubber elongation factor).
    J Allergy Clin Immunol 1996;98(3):640-51
  21. Chardin H, Raulf-Heimsoth M, Chen Z, Rihs HP, Mayer C, Desvaux FX, Senechal H, Peltre G. Interest of two-dimensional electrophoretic analysis for the characterization of the individual sensitization to latex allergens. Int Arch Allergy Immunol 2002;128(3):195-203
  22. Poulos LM, O’Meara TJ, Hamilton RG, Tovey ER. Inhaled latex allergen (Hev b 1).
    J Allergy Clin Immunol 2002;109(4):701-6
  23. Durauer A, Csaszar E, Mechtler K, Jungbauer A, Schmid E. Characterisation of the rubber elongation factor from ammoniated latex by electrophoresis and mass spectrometry.
    J Chromatogr A 2000;890(1):145-58
  24. Chen Z, Cremer R, Posch A, Raulf-Heimsoth M, Rihs HP, Baur X. On the allergenicity of Hev b 1 among health care workers and patients with spina bifida allergic to natural rubber latex.
    J Allergy Clin Immunol 1997;100(5):684-93
  25. Alenius H, Kalkkinen N, Yip E, Hasmin H, Turjanmaa K, Makinen-Kiljunen S, Reunala T, Palosuo T. Significance of rubber elongation factor as a latex allergen. Int Arch Allergy Immunol 1996;109(4):362-8
  26. Bohle B, Wagner B, Vollmann U, Buck D, Niggemann B, Szepfalusi Z, Fischer G, Scheiner O, Breiteneder H, Ebner C. Characterization of T cell responses to Hev b 3, an allergen associated with latex allergy in spina bifida patients.
    J Immunol 2000;164(8):4393-8
  27. Wagner B, Krebitz M, Buck D, Niggemann B, Yeang HY, Han KH, Scheiner O, Breiteneder H. Cloning, expression, and characterization of recombinant Hev b 3, a Hevea brasiliensis protein associated with latex allergy in patients with spina bifida. J Allergy Clin Immunol 1999;104(5):1084-92
  28. Baur X, Chen Z, Rozynek P, Duser M, Raulf Heimsoth M. Cross-reacting IgE antibodies recognizing latex allergens, including Hev b 1, as well as papain. Allergy 1995;50(7):604-9
  29. Oh SK, Kang H, Shin DH, Yang J, Chow KS, Yeang HY, Wagner B, Breiteneder H, Han KH. Isolation, characterization, and functional analysis of a novel cDNA clone encoding a small rubber particle protein from Hevea brasiliensis. J Biol Chem 1999 Jun 11;274(24):17132-8
  30. Yeang HY, Ward MA, Zamri AS, Dennis MS, Light DR. Amino acid sequence similarity of Hev b 3 to two previously reported 27- and 23-kDa latex proteins allergenic to spina bifida patients. Allergy 1998;53(5):513-9
  31. Beezhold DH, Hickey VL, Sussman GL. Mutational analysis of the IgE epitopes in the latex allergen Hev b 5. J Allergy Clin Immunol 2001;107(6):1069-76
  32. Slater JE, Vedvick T, Arthur Smith A, Trybul DE, Kekwick RG. Identification, cloning, and sequence of a major allergen (Hev b 5) from natural rubber latex (Hevea brasiliensis).
    J Biol Chem 1996;271(41):25394-9
  33. Sutherland MF, Drew A, Rolland JM, Slater JE, Suphioglu C, O’Hehir RE. Specific monoclonal antibodies and human immunoglobulin E show that Hev b 5 is an abundant allergen in high protein powdered latex gloves.
    Clin Exp Allergy 2002;32(4):583-9
  34. de Silva HD, Sutherland MF, Suphioglu C, McLellan SC, Slater JE, Rolland JM, O’hehir RE. Human T-cell epitopes of the latex allergen Hev b 5 in health care workers. J Allergy Clin Immunol 2000;105(5):1017-24
  35. Beezhold DH, Hickey VL, Sutherland MF, O’Hehir RE. The Latex allergen Hev b 5 Is an antigen with repetitive murine B-cell epitopes. Int Arch Allergy Immunol 2004;134(4):334-40
  36. Beezhold DH, Hickey VL, Slater JE, Sussman GL. Human IgE-binding epitopes of the latex allergen Hev b 5. J Allergy Clin Immunol 1999;103(6):1166-72
  37. Lundberg M, Chen Z, Rihs HP, Wrangsjo K. Recombinant spiked allergen extract.
    Allergy 2001;56(8):794-5
  38. Akasawa A, Hsieh LS, Martin BM, Liu T, Lin Y. A novel acidic allergen, Hev b 5, in latex. Purification, cloning and characterization.
    J Biol Chem 1996;271(41):25389-93
  39. Fowler MR, Gartland J, Norton W, Slater A, Elliott MC, Scott NW. RS2: a sugar beet gene related to the latex allergen Hev b 5 family.
    J Exp Bot 2000;51(353):2125-6
  40. Rozynek P, Posch A, Baur X. Cloning, expression and characterization of the major latex allergen prohevein.
    Clin Exp Allergy 1998;28(11):1418-26
  41. Raulf-Heimsoth M, Rozynek P, Bruning T, Rihs HP. Characterization of B- and T-cell responses and HLA-DR4 binding motifs of the latex allergen Hev b 6.01 (prohevein) and its post-transcriptionally formed proteins
    Hev b 6.02 and Hev b 6.03.
    Allergy 2004;59(7):724-33
  42. de Silva HD, Gardner LM, Drew AC, Beezhold DH, Rolland JM, O’Hehir RE. The hevein domain of the major latex-glove allergen Hev b 6.01 contains dominant T cell reactive sites.
    Clin Exp Allergy 2004;34(4):611-8
  43. Yeang HY, Arif SA, Yusof F, Sunderasan E. Allergenic proteins of natural rubber latex. Methods 2002;27(1):32-45
  44. Drew AC, Eusebius NP, Kenins L, de Silva HD, Suphioglu C, Rolland JM, O’hehir RE. Hypoallergenic variants of the major latex allergen Hev b 6.01 retaining human T lymphocyte reactivity.
    J Immunol 2004;173(9):5872-9
  45. Alenius H, Kalkkinen N, Reunala T, Turjanmaa K, Palosuo T. The main IgE-binding epitope of a major latex allergen, prohevein, is present in its N-terminal 43-amino acid fragment, hevein.
    J Immunol 1996;156(4):1618-25
  46. Posch A, Wheeler CH, Chen Z, Flagge A, Dunn MJ, Papenfuss F, Raulf-Heimsoth M, Baur X. Class I endochitinase containing a hevein domain is the causative allergen in latex-associated avocado allergy.
    Clin Exp Allergy 1999;29(5):667-72
  47. Karisola P, Kotovuori A, Poikonen S, Niskanen E, Kalkkinen N, Turjanmaa K, Palosuo T, Reunala T, Alenius H, Kulomaa MS. Isolated hevein-like domains, but not 31-kDa endochitinases, are responsible for IgE-mediated in vitro and in vivo reactions in latex-fruit syndrome. J Allergy Clin Immunol 2005;115(3):598-605
  48. Diaz-Perales A, Blanco C, Sanchez-Monge R, Varela J, Carrillo T, Salcedo G. Analysis of avocado allergen (Prs a 1) IgE-binding peptides generated by simulated gastric fluid digestion. J Allergy Clin Immunol 2003;112(5):1002-7
  49. Mikkola JH, Alenius H, Kalkkinen N, Turjanmaa K, Palosuo T, Reunala T. Hevein-like protein domains as a possible cause for allergen cross-reactivity between latex and banana. J Allergy Clin Immunol 1998;102(6 Pt 1):1005-12
  50. Raulf-Heimsoth M, Stark R, Sander I, Maryska S, Rihs HP, Bruning T, Voshaar T. Anaphylactic reaction to apple juice containing acerola: cross-reactivity to latex due to prohevein.
    J Allergy Clin Immunol 2002;109(4):715-6
  51. Karisola P, Mikkola J, Kalkkinen N, Airenne KJ, Laitinen OH, Repo S, Pentikainen OT, Reunala T et al. Construction of hevein (Hev b 6.02) with reduced allergenicity for immunotherapy of latex allergy by comutation of six amino acid residues on the conformational IgE epitopes.
    J Immunol 2004;172(4):2621-8
  52. Laukkanen ML, Makinen-Kiljunen S, Isoherranen K, Haahtela T, Soderlund H, Takkinen K. Hevein-specific recombinant IgE antibodies from human single-chain antibody phage display libraries.
    J Immunol Methods 2003;278(1-2):271-81
  53. Chen Z, Posch A, Cremer R, Raulf-Heimsoth M, Baur X Identification of hevein (Hev b 6.02) in Hevea latex as a major cross-reacting allergen with avocado fruit in patients with latex allergy.
    J Allergy Clin Immunol 1998;102(3):476-81
  54. Reyes-Lopez CA, Hernandez-Santoyo A, Pedraza-Escalona M, Mendoza G, Hernandez-Arana A, Rodriguez-Romero A. Insights into a conformational epitope of Hev b 6.02 (hevein). Biochem Biophys Res Commun 2004;314(1):123-30
  55. Chen Z, Posch A, Lohaus C, Raulf-Heimsoth M, Meyer HE, Baur X. Isolation and identification of hevein as a major IgE-binding polypeptide in Hevea latex.
    J Allergy Clin Immunol 1997;99(3):402-9
  56. Nieto A, Mazon A, Boquete M, Carballada F, Asturias JA, Martinez J, Martinez A. Assessment of profilin as an allergen for latex-sensitized patients.
    Allergy 2002;57(9):776-84
  57. Ganglberger E, Radauer C, Wagner S, Riordain G, Beezhold DH  et al. Hev b 8, the Hevea brasiliensis latex profilin, is a cross-reactive allergen of latex, plant foods and pollen. Int Arch Allergy Immunol 2001;125(3):216-27
  58. Rihs HP, Chen Z, Rozynek P, Baur X, Lundberg M, Cremer R. PCR-based cloning, isolation, and IgE-binding properties of recombinant latex profilin (rHev b 8).
    Allergy 2000;55(8):712-7
  59. Wagner S, Radauer C, Hafner C, Fuchs H, Jensen-Jarolim E, Wuthrich B, Scheiner O, Breiteneder H. Characterization of cross-reactive bell pepper allergens involved in the latex-fruit syndrome.
    Clin Exp Allergy 2004;34(11):1739-46
  60. Vallier P, Balland S, Harf R, Valenta R, Deviller P. Identification of profilin as an IgE-binding component in latex from Hevea brasiliensis: clinical implications.
    Clin Exp Allergy 1995;25(4):332-9
  61. Reindl J, Rihs HP, Scheurer S, Wangorsch A, Haustein D, Vieths S. IgE reactivity to profilin in pollen-sensitized subjects with adverse reactions to banana and pineapple. Int Arch Allergy Immunol 2002;128(2):105-14
  62. Barderas R, Villalba M, Rodriguez R. Recombinant expression, purification and cross-reactivity of chenopod profilin: rChe a 2 as a good marker for profilin sensitization. Biol Chem 2004;385(8):731-7
  63. Ye Q, Xu Y, Yan F, Tang L, Chen F. Molecular cloning and characterization of rice pollen profilin. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai) 2001;33(4):452-6
  64. Wagner S, Breiteneder H, Simon-Nobbe B, Susani M, Krebitz M, Niggemann B et al.
    Hev b 9, an enolase and a new cross-reactive allergen from hevea latex and molds. Purification, characterization, cloning and expression.
    Eur J Biochem 2000;267(24):7006-7014
  65. Rihs HP, Dumont B, Rozynek P, Lundberg M, Cremer R, Bruning T, Raulf-Heimsoth M. Molecular cloning, purification, and IgE-binding of a recombinant class I chitinase from Hevea brasiliensis leaves (rHev b 11.0102). Allergy 2003;58(3):246-51
  66. O’Riordain G, Radauer C, Hoffmann-Sommergruber K, Adhami F et al. Cloning and molecular characterization of the Hevea brasiliensis allergen Hev b 11, a class I chitinase.
    Clin Exp Allergy 2002;32(3):455-62
  67. Diaz-Perales A, Collada C, Blanco C, Sanchez-Monge R et al. Cross-reactions in the latex-fruit syndrome: A relevant role of chitinases but not of complex asparagine-linked glycans. J Allergy Clin Immunol 1999;104(3 Pt 1):681-7
  68. Kespohl S, Sander I, Merget R, Petersen A, Meyer HE, Sickmann A, Bruening T, Raulf-Heimsoth M. Identification of an obeche (Triplochiton scleroxylon) wood allergen as a class I chitinase.
    Allergy 2005;60(6):808-14
  69. Fujimura T, Shigeta S, Suwa T, Kawamoto S, Aki T, Masubuchi M, Hayashi T, Hide M, Ono K. Molecular cloning of a class IV chitinase allergen from Japanese cedar (Cryptomeria japonica) pollen and competitive inhibition of its immunoglobulin E-binding capacity by latex C-serum.
    Clin Exp Allergy 2005;35(2):234-43