[Identification of potentially invasive species of black flies [Diptera: Simuliidae] from Armenia based on an analysis of variability in the mtDNA barcode of the cox1 gene and chromosomal polymorphism].

Black flies (Diptera, Simuliidae) are well known for their medical, environmental, and veterinary importance. The simuliid fauna of Armenia includes 53 species. A number of dominant species are of ecological importance. Complex analysis, which involved morphometric, cytogenetic, and molecular genetic approaches, was conducted to characterize the species status of black flies inhabiting the territory of Armenia. It was shown that the predominant simuliid species, Simulium paraequinum and Simulium kiritshenkoi, belong to a group of species with minimal variability of the cox1 gene. The recently discovered species, Simulium noellery and Simulium [B.] erythrocephalum, which are new to Armenia, can be considered as potentially invasive, which is supported by the low level of variability of the cox1 gene.

Discrete MBL-MASP complexes show wide inter-individual variability in concentration: data from UK vs Armenian populations.

Mannan-binding lectin (MBL) circulates in plasma in complex with MBL-associated serine proteases (MASP) -1, -2 and -3 and a smaller component, MAp19. When MBL binds to the surface of foreign material (microorganisms), MASP-1, -2, -3 are activated. MASP-2 then activates the complement system. MASP-1 and -3 may activate other (unidentified) systems. MBL levels, MBL-bound MASP-1 and MBL-bound MASP-2 activities have been evaluated in healthy individuals from UK and Armenian populations. MBL-bound MASP-2 activity declines in aging (P<0.04). MBL correlates with smoking (P<0.02). There were significant differences between the two populations in MBL-bound MASP-1 activity and in MBL, but no difference in MBL-bound MASP-2 activity. When MASP activities were normalised to MBL (i.e. MASP-1 activity/MBL, MASP-2 activity/MBL), normalised MASP-2 activity in UK individuals was more than 2 fold higher than in Armenians. The difference in normalised MASP-2 activity level between these two Caucasoid populations, suggests that concentration of the MBL-(MASP-2) complex, and therefore the function of activating complement, depends not only on the quantity of MBL in serum and its oligomeric state, but also on the quantity of MASP-2 in serum. It is likely that in individuals with high MBL concentration there is excess free MBL not occupied by MASPs, particularly not by MASP-2.

Collectins and host defence.

The collectins are a small family of soluble oligomeric proteins containing collagenous regions and C-type lectin domains. They are related in structure and function to complement protein C1q, and to H-, L- and M-ficolins. In humans, the collectins mannose-binding lectin (MBL) and surfactant proteins A and D (SP-A, SP-D) have important roles in innate immunity. MBL occurs mainly in blood plasma and in the upper respiratory tract. It binds to neutral sugar arrays on microorganisms and acts as an opsonin either directly (by binding to cell-surface calreticulin) or indirectly by activating complement. MBL circulates in complex with any of three proteases, named MBL-associated serine proteases (MASPs)-1, -2 and -3. MBL-MASP-2 complexes activate complement, but the role of MBL-MASP-1 and MBL-MASP-3 complexes is not yet known. MBL deficiency occurs at high frequency, and is associated with susceptibility to infection, particularly in infants. SP-A and SP-D are most abundant in the lungs, and also bind to microorganisms and inhaled particulates, mainly by lectin-sugar interactions. They do not activate complement, but act as opsonins and agglutinators, and have additional effects on cellular regulation. Mice deficient in SP-A or SP-D are susceptible to lung infections, and SP-D-deficient mice develop an emphysema-like condition.