Developmentally regulated expression of a unique small heat shock protein in Brugia malayi
| Autor: | Diana V. Pastrana, Ward Eisinger, Alan L. Scott, Nithyakalyani Raghavan, Inca Ghosh |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
DNA
Complementary Blotting Western Molecular Sequence Data Brugia malayi Nitric oxide Mice chemistry.chemical_compound Complementary DNA Heat shock protein Animals Parasite hosting Amino Acid Sequence Molecular Biology Heat-Shock Proteins Mice Inbred BALB C biology Reverse Transcriptase Polymerase Chain Reaction Gene Expression Regulation Developmental Helminth Proteins Sequence Analysis DNA biology.organism_classification Immunohistochemistry Molecular biology Oxidative Stress Open reading frame Nematode chemistry Female Parasitology Heat-Shock Response Homeostasis Molecular Chaperones |
| Zdroj: | Molecular and Biochemical Parasitology. 104:233-246 |
| ISSN: | 0166-6851 |
| DOI: | 10.1016/s0166-6851(99)00150-4 |
| Popis: | A screen of an expression library from the fourth larval stage (L4) of the parasitic nematode Brugia malayi resulted in the identification of a 727 bp full-length cDNA with 29–40% identity to members of the small heat shock family of proteins ( Bm - hsp -s1). The open reading frame encoded a protein of approximately 18 kDA ( Bm -HSP-s1). An alignment of the Bm -HSP-s1 sequence with the sequences of small HSPs from vertebrate and invertebrate species demonstrated that a majority of the identity was concentrated in the central α-crystallin domain. Bm -HSP-s1 was constitutively produced by L4 and adult parasites and at low levels by third-stage larvae (L3), but not by first-stage larvae (microfilariae). In adult parasites, Bm -HSP-s1 was localized to the body wall muscle cells and to the cells of the hypodermis/lateral cord. Bm -HSP-s1 production was induced in adult and L3 incubated at 42°C and in L3s during the developmental transition from vector-stage to vertebrate-stage parasites at 37°C. Neither increased nor decreased temperatures induced Bm -HSP-s1 production in microfilariae. Nitric oxide induced low-level, transient Bm -HSP-s1 synthesis in adults, but not in microfilariae. Bm -HSP-s1 did not function as a molecular chaperone to prevent heat-induced aggregation of a test substrate. The developmentally regulated expression and inducable nature of Bm -HSP-s1 suggests that it may have a stage-restricted role in maintaining parasite homeostasis. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect