Expression of small heat shock proteins by the third-stage larva of Brugia pahangi

• Published in: Molecular and biochemical parasitology Vol. 56; no. 2; pp. 219 - 226
• Main Authors: Jecock, Rowena M., Devaney, Eileen
• Format: Journal Article
• Language: English
• Published: Shannon Elsevier B.V 01.12.1992; Elsevier Science
• Subjects: Aedes - parasitology; Animals; Biochemistry. Physiology. Immunology. Molecular biology; Biological and medical sciences; Brugia pahangi; Brugia pahangi - growth & development; Brugia pahangi - metabolism; Fundamental and applied biological sciences. Psychology; Gerbillinae - parasitology; Heat-Shock Proteins - biosynthesis; Helminth Proteins - biosynthesis; Host-Parasite Interactions; Infective L 3; Invertebrates; Larva - metabolism; Nemathelminthia. Plathelmintha; Physiology. Development; Small heat shock protein; Temperature shift; Time Factors; Tropical medicine; Infective L 3; HSP; Brugia pahangi; NEPHGE; FBS; NP-40; 2-D; DOC; Small heat shock protein; Temperature shift; p.i; L 3; Regulation(control); Temperature; Protein synthesis; Heat shock protein; Helmintha; Environmental factor; Nemathelminthia; Developmental stage; Invertebrata; Nematoda
• ISSN: 0166-6851; 1872-9428
• DOI: 10.1016/0166-6851(92)90171-F

Changes in proteins synthesised by the infective third-stage larvae (L 3) of the filarial nematode Brugia pahangi were examined with respect to the temperature shift encountered by the parasite as it migrates from insect to mammal, and the presence of serum in the culture medium. While the synthesis of a number of polypeptides is regulated by the temperature shift of the L 3 from 28°C to 37°C in vitro, there is no evidence that serum has any significant effect on protein synthesis. Two complexes of small acidic polypeptides (22–24 kDa and 18 kDa) are synthesised for a limited period only by L 3 transferred to 37°C. One component of each complex appears to be constitutively expressed at 28°C, but its synthesis is up-regulated at 37°C, while the remaining members of each complex are synthesised only at 37°C. Subjection of L 3 and post-infective (p.i.) L 3 to heat shock (41°C) also induces synthesis of both complexes, indicating that these heat-inducible polypeptides are related to the family of small heat shock proteins. The possible role of the heat shock-related proteins in this important environmental transition is considered.