Ultrastructural localization of Ani s 1, a major allergen from the fish parasite Anisakis simplex.
No data about the nature or function of the first major Anisakis simplex allergen, named Ani s 1, is available. The aim of this study was to investigate the ultrastructural localization of this protein, to obtain further information about it. Ani s 1 was detected in secretory granules of the excretory gland and occasionally lining the main excretory canal. Our results suggest that Ani s 1 could be a secretory product and could have an enzymatic function related to mechanisms of infection.
Gómez-Aguado
F
F
Department of Pathology, Carlos III Hospital, Sinesio Delgado 10, 28029 Madrid, Spain. fgomez.hciii@madrid.salud.org
Picazo
A
A
Caballero
M L
ML
Moneo
I
I
Asturias
J A
JA
Corcuera
M T
MT
Casado
I
I
Alonso
M J
MJ
D000485:Allergens / Q000032:analysis* / Q000276:immunology; D000818:Animals; D017129:Anisakiasis / Q000469:parasitology / Q000662:veterinary*; D017163:Anisakis / Q000737:chemistry / Q000276:immunology* / Q000648:ultrastructure*; D002135:Calcium-Binding Proteins / Q000032:analysis* / Q000276:immunology; D005393:Fish Diseases / Q000469:parasitology*; D005399:Fishes; D015801:Helminth Proteins / Q000032:analysis* / Q000276:immunology / Q000302:isolation & purification; D006790:Host-Parasite Interactions; D006801:Humans; D008297:Male; D011817:Rabbits; D022142:Secretory Vesicles / Q000648:ultrastructure
D000485:Allergens; D002135:Calcium-Binding Proteins; D015801:Helminth Proteins; C412511:troponin-like protein, Anisakis simplex