title: Fusarium solani major allergen peptide IV-1 binds IgE but does not release histamine.
abstract: BACKGROUND
  Fusarium solani (FS) is an important allergen source afflicting 4% of the nasobronchial allergy patients. Fus s I3596*, a 65 kDa major glycoprotein allergen of FS reacts with 95% fungus sensitive patients.
  
  
  OBJECTIVE
  To purify and characterize a potent peptide from Fus s I3596* which may be useful for therapeutic purposes.
  
  
  METHODS
  The 65 kDa protein was sequentially cleaved with trypsin and cyanogen bromide (CNBr). The cleaved products were purified on reverse phase high performance liquid chromatography (rpHPLC) column and functionally characterized by in vitro and in vivo methods for its IgE binding and histamine release.
  
  
  RESULTS
  The protein on cleavage showed 11 peaks (I to XI). Of these, peaks I, III, IV and V were highly allergenic as determined by IgE ELISA. These peaks were further purified and peptide IV-1 was most potent in comparison to other peptides by ELISA-inhibition. This peptide showed IgE binding but could not evoke intradermal response in Fusarium-sensitive patients. Heparinized blood challenged with peptide IV-1 does not release histamine. Preincubation of heparinized blood with peptide IV-1 and challenging with crude extract blocked histamine release in a dose dependent manner.
  
  
  CONCLUSIONS
  Peptide IV-1 binds to IgE but does not release histamine, demonstrating its potential use in therapy of Fusarium-allergic patients.
authors: Allergy & Immunology Section, Centre for Biochemical Technology, Mall Road, Delhi, India.
authors: J
authors: J
authors: Verma
authors: S
authors: S
authors: Sridhara
authors: B P
authors: BP
authors: Singh
authors: S
authors: S
authors: Pasha
authors: S V
authors: SV
authors: Gangal
authors: N
authors: N
authors: Arora
mesh_terms: D000328:Adult; D000485:Allergens / Q000302:isolation & purification / Q000378:metabolism*; D000925:Anticoagulants / Q000494:pharmacology; D000946:Antigens, Fungal / Q000302:isolation & purification / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D003488:Cyanogen Bromide / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D005670:Fusarium / Q000276:immunology*; D006023:Glycoproteins / Q000302:isolation & purification / Q000378:metabolism*; D006493:Heparin / Q000494:pharmacology; D006636:Histamine Release / Q000502:physiology*; D006801:Humans; D007073:Immunoglobulin E / Q000378:metabolism*; D007074:Immunoglobulin G / Q000737:chemistry; D008970:Molecular Weight; D010446:Peptide Fragments / Q000302:isolation & purification / Q000378:metabolism* / Q000494:pharmacology; D011485:Protein Binding; D017455:Receptors, IgE / Q000187:drug effects; D012680:Sensitivity and Specificity; D014357:Trypsin / Q000494:pharmacology
chemical_list: D000485:Allergens; D000925:Anticoagulants; D000946:Antigens, Fungal; D006023:Glycoproteins; D007074:Immunoglobulin G; D010446:Peptide Fragments; D017455:Receptors, IgE; D007073:Immunoglobulin E; D006493:Heparin; D014357:Trypsin; D003488:Cyanogen Bromide