Protein components of homogenates of unfed larvae and nymphs of Ixodes ricinus (L.), and of ovary, haemolymph, Malpighian tubules, rectal ampulla, fat body, integument, salivary glands and midgut of partially fed adult females were studied for their antigenicity and carbohydrate moieties using immunoblotting and lectin affinity blotting (LAB) techniques. Comparing the individual anti-larval, anti-nymphal and anti-adult immune sera for their capacity to recognize the specific and trans-stadially cross-reactive antigenic proteins, larval feeding induced the most effective humoral response. The majority of immunogens recognized by rabbit anti-tick immune sera are glycoproteins. Most of the glycosylated antigens were modified with N-type glycans; however, O-type glycans were also demonstrated in some antigens. The correlation of the type of glycosylation with antigenicity, and the sharing of common antigenic epitopes by various tissues, are discussed.

The effect of repeated infestations of Ixodes ricinus (L.) nymphs on BALB/c mice was studied. Four successive infectations resulted in an increase of tick feeding success. Tick yield and mean engorged weight increased and the length of the feeding period was reduced significantly (P < 0.05-0.01). The increase of specific anti-tick antibodies was not significant (P > 0.05). The blastogenic response of spleen lymphocytes to T-cell mitogens (Con A and PHA-P) was unimpaired or slightly enhanced, whereas the response to B-cell activators (LPS and PWM) was suppressed, as was the total antibody generation in vitro. The numbers of mast cells in murine skin at the tick attachment sites slightly decreased during the third infestation. The suppression of B-cell competence and of antibody generation, together with decrease of skin mast cell numbers in tick attachment sits, are considered to be responsible for enhancement of tick feeding success.

Lectins have been suggested to function as pattern-recognition molecules in invertebrate immune mechanisms. A lectin from the hemolymph of the tick Ixodes ricinus with main specificity for sialic acid was characterized and antibodies directed against this lectin were prepared. In this study, these antibodies were used to localize the lectin in the tissues of I. ricinus. Immunoreactivity with poly- and monoclonal antibodies was detected in the granules of both types of granular hemocytes, at the membrane of hemocytes, and at the basal laminae surrounding the hemocoel. Furthermore, cells attached to the midgut, invaginations of Géné's organ, and granular inclusions of nephrocytes were labeled. The immunoreactivity detected in hemocytes and the hemocoel lining supports the idea that the hemolymph lectin may function as a recognition molecule in the immune system of I. ricinus. Another function could be protection of eggs that are coated with secretions by Géné's organ. The lectin activity could also be involved in transmission of Borrelia burgdorferi, the causative agent of Lyme borreliosis, and the tick-borne encephalitis virus.

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