The sialotranscriptome of Antricola delacruzi female ticks is compatible with non-hematophagous behavior and an alternative source of food.
The hosts for Antricola delacruzi ticks are insectivorous, cave-dwelling bats on which only larvae are found. The mouthparts of nymphal and adult A. delacruzi are compatible with scavenging feeding because the hypostome is small and toothless. How a single blood meal of a larva provides energy for several molts as well as for oviposition by females is not known. Adults of A. delacruzi possibly feed upon an unknown food source in bat guano, a substrate on which nymphal and adult stages are always found. Guano produced by insectivorous bats contains twice the amount of protein and 60 times the amount of iron as beef. In addition, bacteria and chitin-rich fungi proliferate on guano. Comparative data on the transcriptome of the salivary glands of A. delacruzi is nonexistent and would help to understand the physiological adaptations of salivary glands that accompany different sources of food as well as the steps taken by the Acari toward haematophagy, believed to have evolved from scavenging dead animals. Annotation of the transcriptome of salivary glands from female instars of A. delacruzi collected on guano categorized 5.7% of the clusters of expressed genes as putative secreted proteins. They included abundantly expressed TIL-domain-containing proteins (possible anti-microbials), an abundantly expressed protein similar to a serum amyloid found in the sialotranscriptomes of Ornithodoros spp., a savignygrin, a family of mucin/peritrophin/cuticle-like proteins, anti-microbials and an HIV envelope-like glycoprotein also found in soft ticks. When comparing the transcriptome of A. delacruzi with those of blood-feeding female soft and hard ticks some notable differences were observed; they consisted of the following transcripts over- or under-represented or absent in the sialotranscriptome of A. delacruzi that may reflect its source of food: ferritin, mucins with chitin-binding domains and TIL-domain-containing proteins versus lipocalins, basic tail proteins, metalloproteases, glycine-rich proteins and Kunitz protease inhibitors, respectively.
Laboratory of Malaria and Vector Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD, USA.
José Marcos C
JM
Ribeiro
Marcelo B
MB
Labruna
Ben J
BJ
Mans
Sandra Regina
SR
Maruyama
Ivo M B
IM
Francischetti
Gustavo Canavaci
GC
Barizon
Isabel K F
IK
de Miranda Santos
D000222:Adaptation, Physiological; D000595:Amino Acid Sequence; D000818:Animals; D026862:Argasidae / Q000235:genetics / Q000378:metabolism*; D002685:Chiroptera / Q000469:parasitology; D005243:Feces; D005247:Feeding Behavior; D005260:Female; D020869:Gene Expression Profiling; D015723:Gene Library; D020043:Genes, Essential; D049810:Genetic Speciation; D008969:Molecular Sequence Data; D012463:Saliva / Q000378:metabolism*; D012469:Salivary Glands / Q000378:metabolism; D059467:Transcriptome