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 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]Galleria melonella responds to
caffeine intake by increased Hemolin protein expression.[12]
Hemolin is thought to be a gene duplication of the developmental protein neuroglian,[13] 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,[14] and is induced during diapause and by
20-Hydroxyecdysone in Lymantria dispar.[15]RNAi of Hemolin causes malformation in H. cecropia.[16]
^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.
PMID1790333.
^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.
PMID9703515.
^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.
PMID15978282.
^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.
PMID9818384.
^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.
PMID17126583.
^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.
PMID17981330.
^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.
PMID9472064.
S2CID36390766.
^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.
PMID12530213.
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 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]Galleria melonella responds to
caffeine intake by increased Hemolin protein expression.[12]
Hemolin is thought to be a gene duplication of the developmental protein neuroglian,[13] 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,[14] and is induced during diapause and by
20-Hydroxyecdysone in Lymantria dispar.[15]RNAi of Hemolin causes malformation in H. cecropia.[16]
^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.
PMID1790333.
^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.
PMID9703515.
^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.
PMID15978282.
^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.
PMID9818384.
^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.
PMID17126583.
^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.
PMID17981330.
^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.
PMID9472064.
S2CID36390766.
^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.
PMID12530213.