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ARS Home » Plains Area » Kerrville, Texas » Knipling-Bushland U.S. Livestock Insects Research Laboratory » LAPRU » Research » Publications at this Location » Publication #346796
Title: Functional and morphological analysis of putative chemoreception-related proteins in the lone star tick, Amblyomma americanum

Author
item TRIVEDI, P - University Of Texas At San Antonio
item DAS, T - University Of Texas At San Antonio
item BACH, S - University Of Texas At San Antonio
item SESHU, J - University Of Texas At San Antonio
item Lohmeyer, Kimberly - Kim
item Perez De Leon, Adalberto - Beto
item RENTHAL, R - University Of Texas At San Antonio

Submitted to: Meeting Abstract
Publication Type: Abstract Only
Publication Acceptance Date: 6/19/2017
Publication Date: N/A
Citation: N/A

Interpretive Summary:

Technical Abstract: Ehrlichiosis, a potentially fatal infection, is caused by rickettsial bacteria transmitted by the lone star tick, Amblyomma americanum. We previously analyzed the chemosensory appendage proteome of A. americanum as part of a project to develop new chemosensory-based vector control methods. Among the chemosensory-related proteins we identified were OBPL1 and OBPL2, predicted to be similar to insect odorant-binding proteins. The A. americanum OBPL1 sequence was incomplete, but the full-length sequence of a highly similar protein was found in the Ixodes scapularis genome. We have now expressed I. scapularis OBPL1 and A. americanum OBPL2 in E. coli and measured the binding of the purified proteins to N-phenylnaphthylamine (NPN), a hydrophobic fluorescent dye known to interact strongly with insect odorant-binding proteins. Both OBPL1 and OBPL2 showed strong, saturable binding to NPN, indicating the presence of a discrete hydrophobic ligand-binding pocket. We also used imaging mass spectrometry to identify proteins in the region of the olfactory Haller's organ on the A. americanum fore tarsus. A protein with a mass-to-charge ratio (m/z) close to 9300 was found uniquely in the vicinity of the DI.1 sensilla, distal to the anterior pit sensilla. One of the most abundant chemosensory-related proteins we previously detected in the fore tarsus proteome was a microplusin-like protein called ML1, with an expected m/z of 9302. This indicates that ML1 could be involved in the olfactory activity of the DI.1 sensilla.