Degradation of haemoglobin in Chironomus during metamorphosis

Schin, Kissu; Poluhowich, John J.; Gamo, Takuma; Laufer, Hans

doi:10.1016/0022-1910(74)90163-2

Cited by 31 publications

(17 citation statements)

References 9 publications

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“…Earlier studies, using in vivo and in vitro testing, showed congruence between antigens of larvae, pu pae and adults of the Sudanese C. lewisi, and between these adults and both larvae and adults of C. thummi [3,8,21], The present study confirms and extends these previous reports and strengthens the observa tions of Schin et al [17,18] that hemoglobin is incom pletely degraded through metamorphosis, although it is excreted into the meconium of the newly emerged adult [13].…”

Section: Discussionsupporting

confidence: 83%

Persistence of Hemoglobin Allergenicity and Antigenicity during Metamorphosis of Chironomidae (Insecta: Diptera)

Prelicz¹,

Baur²,

Dewair³

et al. 1986

Int Arch Allergy Immunol

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Chironomid hemoglobins are potent allergens. The allergenic and antigenic activities of these hemoglobins are studied with the help of RAST, RAST inhibition and double immunodiffusion. Human as well as rabbit antisera were used. It was shown that hemoglobins are the main antigenic/allergenic components in extracts of Camptochironomus tentans larvae. Furthermore, immunological cross-reactivity among larvae, pupae and adult midges of this species are shown to be due to the existence of hemoglobin antigenic determinants in all developmental stages of this insect.

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Section: Discussionsupporting

confidence: 83%

Persistence of Hemoglobin Allergenicity and Antigenicity during Metamorphosis of Chironomidae (Insecta: Diptera)

Prelicz¹,

Baur²,

Dewair³

et al. 1986

Int Arch Allergy Immunol

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“…Mature adult extracts were shown to contain more substances that bound to the IgE of those chironomid allergic subjects (16,17). Hemoglobin, known as a major allergen of chironomids (4,27,30), is known to be degraded during metamorphosis (17,24). Galindo et al have reported that subjects unexposed to midges could have IgE to chironomid hemoglobin (5) and hypersensitivity to these larvae without apparent contact with them (6).…”

Section: Discussionmentioning

confidence: 99%

Molecular Cloning and Characterization of Tropomyosin, a Major Allergen of Chironomus kiiensis , a Dominant Species of Nonbiting Midges in Korea

Jeong

Yum

Lee

et al. 2004

Clin Vaccine Immunol

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Chironomids are widely and abundantly distributed in the vicinity of standing waters. Larvae of Chironomus and some other genera are known to contain hemoglobins, which have been described as a major allergen, and the adults that have no hemoglobins also have been reported to contain allergens. In this study, we tried to establish the role of chironomid allergy and characterize the allergen of Chironomus kiiensis adults. Skin tests using C. kiiensis adult extracts were performed on patients with allergic symptoms. A cDNA library of C. kiiensis adults was screened with C. kiiensis immune mouse sera to identify allergens, and results were confirmed using skin test-positive human sera. Recombinant allergen was expressed in Escherichia coli and purified by affinity chromatography using nickel-nitrilotriacetic acid agarose to investigate its allergenic properties. Out of 275 allergic patients 14.2% showed a positive reaction to C. kiiensis adult crude extracts in the skin test. The tropomyosin was cloned by immunoscreening and expressed in Escherichia coli. C. kiiensis tropomyosin has a high homology at the amino acid level with tropomyosins which were previously known to be allergens in various arthropods (Periplaneta americana, 86.3%; Panulirus stimpson, 78.9%; Dermatophagoides pteronyssinus, 76.5%). Specific immunoglobulin E antibodies reacting to recombinant tropomyosin were detected in 17 (81%) of 21 patients whose skin test results were positive. Cross-reactivity against house dust mites and other insects was noticed with mouse anti-recombinant tropomyosin immune serum. C. kiiensis adults were shown to be an important source of inhalant allergens in Korea. Molecular cloning of C. kiiensis tropomyosin was performed and IgE reactivity was demonstrated using skin test-positive human sera. Recombinant tropomyosin will be useful for further studies or clinical applications.

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“…The fa t body is the major site of synthesis (129,389). In metamorphosis, hemoglobin is largely destroyed before emergence of the adult, and the midgut has been invoked as a site of degradation (390,391). Mechanisms for developmental regulation of the synthesis and degradation of this protein must therefore exist.…”

Section: Hemoglobinsmentioning

confidence: 99%