Hemolin

Hemolin is an immunoglobulin-like protein exclusively found in Lepidoptera (moths and butterflies). It was first discovered in immune-challenged pupae of Hyalophora cecropia[1] and Manduca sexta.[2]

Hemolin has a horseshoe crystal structure[3] with four domains and resembles the developmental protein neuroglian.

Hemolin from Hyalophora cecropia superimposed on neuroglian. Predicted differences between the proteins are highlighted in red. Made in Swiss Protein Database Viewer.

Hemolin increases 18-fold up to 7 mg/ml following injection of bacteria in H. cecropia. Induction of Hemolin in moths after bacterial injection have been shown in several species including Antheraea pernyi,[4] Bombyx mori, Helicoverpa zea,[5] Heliothis virescens,[6] Hyphantria cunea,[7] and Samia cynthia.[8]

Hemolin has also been suggested to participate in the immune response to virus infection[9] and shown to bind to virus particles.[10] It is expressed in response to dsRNA in a dose-dependent manner.[11]

Hemolin is thought to be a gene duplication of the developmental protein neuroglian,[12] but has lost two of the protein domains that neuroglian contains. In the potential function as a developmental protein, Hemolin has been shown to increase close to pupation in Manduca sexta,[13] and is induced during diapause and by 20-Hydroxyecdysone in Lymantria dispar.[14] RNAi of Hemolin causes malformation in H. cecropia.[15]

See also

References

  1. ↑ Faye, I; Pye, A; Rasmuson, T; Boman, HG; Boman, IA (December 1975). "Insect immunity. 11. Simultaneous induction of antibacterial activity and selection synthesis of some hemolymph proteins in diapausing pupae of Hyalophora cecropia and Samia cynthia.". Infection and immunity. 12 (6): 1426–38. PMID 812827.
  2. ↑ Ladendorff, NE; Kanost, MR (1991). "Bacteria-induced protein P4 (hemolin) from Manduca sexta: a member of the immunoglobulin superfamily which can inhibit hemocyte aggregation.". Archives of insect biochemistry and physiology. 18 (4): 285–300. doi:10.1002/arch.940180410. PMID 1790333.
  3. ↑ Su, XD; Gastinel, LN; Vaughn, DE; Faye, I; Poon, P; Bjorkman, PJ (Aug 14, 1998). "Crystal structure of hemolin: a horseshoe shape with implications for homophilic adhesion.". Science. 281 (5379): 991–5. doi:10.1126/science.281.5379.991. PMID 9703515.
  4. ↑ Li, W; Terenius, O; Hirai, M; Nilsson, AS; Faye, I (2005). "Cloning, expression and phylogenetic analysis of Hemolin, from the Chinese oak silkmoth, Antheraea pernyi.". Developmental and comparative immunology. 29 (10): 853–64. doi:10.1016/j.dci.2005.02.003. PMID 15978282.
  5. ↑ Terenius, O; Popham, HJ; Shelby, KS (November 2009). "Bacterial, but not baculoviral infections stimulate Hemolin expression in noctuid moths.". Developmental and comparative immunology. 33 (11): 1176–85. doi:10.1016/j.dci.2009.06.009. PMID 19540262.
  6. ↑ Terenius, O; Popham, HJ; Shelby, KS (November 2009). "Bacterial, but not baculoviral infections stimulate Hemolin expression in noctuid moths.". Developmental and comparative immunology. 33 (11): 1176–85. doi:10.1016/j.dci.2009.06.009. PMID 19540262.
  7. ↑ Shin, SW; Park, SS; Park, DS; Kim, MG; Kim, SC; Brey, PT; Park, HY (November 1998). "Isolation and characterization of immune-related genes from the fall webworm, Hyphantria cunea, using PCR-based differential display and subtractive cloning.". Insect biochemistry and molecular biology. 28 (11): 827–37. doi:10.1016/s0965-1748(98)00077-0. PMID 9818384.
  8. ↑ Bao, Y; Yamano, Y; Morishima, I (January 2007). "Induction of hemolin gene expression by bacterial cell wall components in eri-silkworm, Samia cynthia ricini.". Comparative Biochemistry and Physiology B. 146 (1): 147–51. doi:10.1016/j.cbpb.2006.10.092. PMID 17126583.
  9. ↑ Terenius, O (2008). "Hemolin-A lepidopteran anti-viral defense factor?". Developmental and comparative immunology. 32 (4): 311–6. doi:10.1016/j.dci.2007.09.006. PMID 17981330.
  10. ↑ Labropoulou, V; Douris, V; Stefanou, D; Magrioti, C; Swevers, L; Iatrou, K (October 2008). "Endoparasitoid wasp bracovirus-mediated inhibition of hemolin function and lepidopteran host immunosuppression.". Cellular microbiology. 10 (10): 2118–28. doi:10.1111/j.1462-5822.2008.01195.x. PMID 18627380.
  11. ↑ Hirai, M; Terenius, O; Li, W; Faye, I (August 2004). "Baculovirus and dsRNA induce Hemolin, but no antibacterial activity, in Antheraea pernyi.". Insect molecular biology. 13 (4): 399–405. doi:10.1111/j.0962-1075.2004.00497.x. PMID 15271212.
  12. ↑ Hughes, AL (March 1998). "Protein phylogenies provide evidence of a radical discontinuity between arthropod and vertebrate immune systems.". Immunogenetics. 47 (4): 283–96. doi:10.1007/s002510050360. PMID 9472064.
  13. ↑ Yu, XQ; Kanost, MR (Nov 1999). "Developmental expression of Manduca sexta hemolin.". Archives of insect biochemistry and physiology. 42 (3): 198–212. doi:10.1002/(sici)1520-6327(199911)42:3<198::aid-arch4>3.0.co;2-g. PMID 10536048.
  14. ↑ Lee, KY; Horodyski, FM; Valaitis, AP; Denlinger, DL (November 2002). "Molecular characterization of the insect immune protein hemolin and its high induction during embryonic diapause in the gypsy moth, Lymantria dispar.". Insect biochemistry and molecular biology. 32 (11): 1457–67. doi:10.1016/s0965-1748(02)00066-8. PMID 12530213.
  15. ↑ Bettencourt, R.; Terenius, O.; Faye, I. (June 2002). "Hemolin gene silencing by ds-RNA injected into Cecropia pupae is lethal to next generation embryos". Insect Molecular Biology. 11 (3): 267–271. doi:10.1046/j.1365-2583.2002.00334.x.
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