Abstract:
:Molecules in the midgut of the tsetse fly (Diptera: Glossinidiae) are thought to play an important role in the life cycle of African trypanosomes by influencing their initial establishment in the midgut and subsequent differentiation events that ultimately affect parasite transmission. It is thus important to determine the molecular composition of the tsetse midgut to aid in understanding disease transmission by these medically important insect vectors. Here, we report that the most abundant protein in the midguts of teneral (unfed) Glossina morsitans morsitans is a 60 kDa molecular chaperone of bacterial origin. Two species of symbiotic bacteria reside in the tsetse midgut, Sodalis glossinidius and Wigglesworthia glossinidia. To determine the exact origin of the 60 kDa molecule, a protein microchemical approach involving two-dimensional (2-D) gel electrophoresis and mass spectrometry was used. Peptide mass maps were compared to virtual peptide maps predicted for S. glossinidius and W. glossinidia 60 kDa chaperone sequences. Four signature peptides were identified, revealing that the source of the chaperone was W. glossinidia. Comparative 2-D gel electrophoresis and immunoblotting further revealed that this protein was localized to the bacteriome and not the distal portion of the tsetse midgut. The possible function of this highly abundant endosymbiont chaperone in the tsetse midgut is discussed.
journal_name
Insect Biochem Mol Bioljournal_title
Insect biochemistry and molecular biologyauthors
Haines LR,Haddow JD,Aksoy S,Gooding RH,Pearson TWdoi
10.1016/s0965-1748(02)00063-2subject
Has Abstractpub_date
2002-11-01 00:00:00pages
1429-38issue
11eissn
0965-1748issn
1879-0240pii
S0965174802000632journal_volume
32pub_type
杂志文章abstract::Methylfarnesoate (MF), an analogue of the insect juvenile hormone III, has been implicated to play a vital role in the regulation of the growth and reproductive development in crustaceans. Farnesoic acid O-methyltransferase (FAMeT) is the key enzyme involved in catalyzing the final step in the MF biosynthetic pathway....
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journal_title:Insect biochemistry and molecular biology
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journal_title:Insect biochemistry and molecular biology
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journal_title:Insect biochemistry and molecular biology
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journal_title:Insect biochemistry and molecular biology
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journal_title:Insect biochemistry and molecular biology
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