Journal of Mosquito Research, 2013, Vol.3, No.4, 21
-
32
ISSN 1927-646X
http://jmr.sophiapublisher.com
31
et al., 2007).
The closest phylogenetic relationship emerged for the
Hymenoptera transferrins (
Apis mellifera
). The
cockroach
B. discoidalis
(Dictyoptera) and the termite
M. darwiniensis
(Isoptera) constitute a well-defined
group this branch is connected to that representing the
Orthoptera (Romalea) all represents hemimetabolous
insects. Even though this molecular tree is exclusively
based on transferrin partial cDNA sequence
information and also includes only eleven insect
species, the species clusters are congruent with
general insect phylogeny. Obviously, the rather
uncertain branching in any part of the tree has to be
attributed to the low number of insect transferrin
sequences available for the comparison.
Molecular phylogenies that include
Cx. quinquefasciatus
are based on single proteins or protein families have
been presented for
Cx. quinquefasciatus
motor
proteins (Odronitz and Kollmar, 2007) diagnostic
enzyme marker MDH (NADP)(Weitzel et al., 2009).
All of these single protein or protein family trees
producing congruent molecular phylogenies, reflected
the evolutionary history of the individual proteins or
protein family members, diagnosed and genetically
separated populations within the
Culex pipiens
complex. This factor is also well represented in the
transferrin tree which shows a clear separation of the
dipteran transferrins from the transferrins of the other
insect orders. The branch within this tree, which is
less well supported, groups the coleopteran
transferrins with hemimetabolous insects. In addition,
our results coincide with the recently published
mosquito transferrin sequence (Paily et al., 2007).
In conclusion, from the present and previous work it
could be suggested that transferrin is an active
component of the mosquito defense system against
invading parasites or pathogens.
Further studies will be necessary to demonstrate
protection afforded by transferrin induction and to link
the transferrin protein titer with transcript levels. This
is especially relevant when we consider the possibility
that pathogen metabolites may interfere with
transferrin gene expression, protein production or
stability through translation control of the expression
of transferrin protein by the bacterial system. The use
of RNA interference to selectively knock down the
transferrin transcript levels may be the most likely
method to achieve this objective.
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