Diagnosis and prevention of food-dependent exercise-induced anaphylaxis
EXPERT REVIEW OF CLINICAL IMMUNOLOGY
Authors: Benito-Garcia, Filipe; Javier Ansotegui, Ignacio; Morais-Almeida, Mario
Abstract
Introduction: Food-dependent, exercise-induced anaphylaxis (FDEIA) is a rare type of anaphylaxis with a growing incidence. Although the precise mechanism by which the patient reacts only in a combination of a culprit food and cofactors are not currently understood, many advances in diagnosis and management have been made since their first description. Areas covered: A literature search in PubMed was performed to review the diagnosis and management of FDEIA. Clinicians should have a high level of suspicion for identification of the culprit foods and the cofactors involved. Component-resolved diagnosis and more accurate provocation tests have revolutionized the diagnosis accuracy. Management is not easy and involves educating the patient to evict the combination of exposure to the culprit foods and the cofactors that elicit anaphylaxis, and how to act and treat if a reaction occurs. Expert opinion: FDEIA is currently misdiagnosed and the authors believe that there are many FDEIA patients labelled as idiopathic anaphylaxis with unnecessary evictions and with a poor quality of life because of the fear of an imminent reaction. Due to recent advances in diagnostic tools and the use of monoclonal antibodies for prophylaxis in persistent cases, FDEIA can have a better prognosis improving the quality of life of the patients and their families.
Preparation and Purification of Recombinant Dipeptidyl Peptidase 4 from Tenebrio molitor
APPLIED BIOCHEMISTRY AND MICROBIOLOGY
Authors: Tereshchenkova, V. F.; Klyachko, E. V.; Benevolensky, S. V.; Belozersky, M. A.; Dunaevsky, Ya. E.; Filippova, I. Yu.; Elpidina, E. N.
Abstract
Dipeptidyl peptidase 4is a unique proline-specific peptidase, capable to hydrolyze the bonds, formed by proline amino acid residue, cleaving dipeptides from N-terminus of peptides and proteins, containing this imino acid in P1 position. Recombinant dipeptidyl peptidase 4 from the insect Tenebrio molitor was prepared for the first time in the Pichia pastoris protein expression system; a method for its purification was proposed. The authenticity of the obtained recombinant enzyme was confirmed by mass spectrometry. The use of the obtained preparation of the T. molitor enzyme is promising for the hydrolysis of resistant to proteolysis proline-rich peptides and proteins, particularly for prolamins - the main storage proteins of cereal seeds, since they are not fully hydrolyzed by human digestive enzymes and cause autoimmune gastrointestinal celiac disease in the susceptible group of people.