Evidence map›Paper›PMID 40234925›Full record

ArticleParasites & vectors2025

Fourteen anti-tick vaccine targets are variably conserved in cattle fever ticks.

Joseph D Busch, Nathan E Stone, Grant L Pemberton, Mackenzie L Roberts, Rebekah E Turner, Natalie B Thornton, Jason W Sahl, Darrin Lemmer, Greta Buckmeier, Sara K Davis and 9 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Parasites & vectors, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

4 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

19 authors.

Joseph D BuschPathogen and Microbiome Institute, Northern Arizona University, 1395 S. Knoles Dr. Bldg 56, Flagstaff, AZ, 86011-4073, USA. Joseph.Busch@nau.edu.
Nathan E StonePathogen and Microbiome Institute, Northern Arizona University, 1395 S. Knoles Dr. Bldg 56, Flagstaff, AZ, 86011-4073, USA.
Grant L PembertonPathogen and Microbiome Institute, Northern Arizona University, 1395 S. Knoles Dr. Bldg 56, Flagstaff, AZ, 86011-4073, USA.
Mackenzie L RobertsPathogen and Microbiome Institute, Northern Arizona University, 1395 S. Knoles Dr. Bldg 56, Flagstaff, AZ, 86011-4073, USA.
Rebekah E TurnerPathogen and Microbiome Institute, Northern Arizona University, 1395 S. Knoles Dr. Bldg 56, Flagstaff, AZ, 86011-4073, USA.
Natalie B ThorntonPathogen and Microbiome Institute, Northern Arizona University, 1395 S. Knoles Dr. Bldg 56, Flagstaff, AZ, 86011-4073, USA.
Jason W SahlPathogen and Microbiome Institute, Northern Arizona University, 1395 S. Knoles Dr. Bldg 56, Flagstaff, AZ, 86011-4073, USA.
Darrin LemmerTGen-North, 3051 W. Shamrell Blvd #106, Flagstaff, AZ, 86005, USA.
Greta BuckmeierUSDA, ARS, KBUSLIRL-LAPRU, 2700 Fredericksburg Rd., Kerrville, TX, 78028-9184, USA.
Sara K DavisUSDA, ARS, ADRU, Washington State University, 3003 ADBF, Pullman, WA, 99164-6630, USA.
Roberto I Guerrero-SolorioImmunology and Vaccine Research Laboratory, Natural Sciences College, Autonomous University of Querétaro, 76230, Querétaro, Mexico.
Shahid KarimSchool of Biological, Environmental, and Earth Sciences, University of Southern Mississippi, 118 College Drive, Hattiesburg, MS, 39406, USA.
Guilherme KlafkeInstituto de Pesquisas Veterinarias Desidério Finamor, Estrada do conde, 6000, Eldorado do sul, 92990-000, Brazil.
Donald B ThomasCattle Fever Tick Research Laboratory, USDA, ARS, Moore Air Base, Building 6419, 22675 N. Moorefield Road, Edinburg, TX, 78541, USA.
Pia U OlafsonUSDA, ARS, KBUSLIRL-LAPRU, 2700 Fredericksburg Rd., Kerrville, TX, 78028-9184, USA.
Massaro UetiUSDA, ARS, ADRU, Washington State University, 3003 ADBF, Pullman, WA, 99164-6630, USA.
Juan MosquedaImmunology and Vaccine Research Laboratory, Natural Sciences College, Autonomous University of Querétaro, 76230, Querétaro, Mexico.
Glen A ScolesUSDA, ARS, IIBBL, Beltsville Agricultural Research Center, 10300 Baltimore Ave., Beltsville, MD, 20705, USA.
David M WagnerPathogen and Microbiome Institute, Northern Arizona University, 1395 S. Knoles Dr. Bldg 56, Flagstaff, AZ, 86011-4073, USA.

Funding

National Institute of Food and Agriculture 2015-67015-23047Northern Arizona University Hooper Undergraduate Research Award (HURA) to R. E. TurnerUSDA-APHIS-VS AP20VSSPRS00C117USDA-ARS NACA 2021 58-2090-1-037USDA-NIFA-AFRI 2018-67015-28301US Department of State Pakistan-US Science and Technology Cooperation Program Award PGA-P21049
6 · The paper itself

Abstract

backgroundRhipicephalus (Boophilus) microplus causes significant cattle production losses worldwide because it transmits Babesia bovis and B. bigemina, the causative agents of bovine babesiosis. Control of these ticks has primarily relied on treatment of cattle with chemical acaricides, but frequent use, exacerbated by the one-host lifecycle of these ticks, has led to high-level resistance to multiple classes of acaricides. Consequently, new approaches for control, such as anti-tick vaccines, are critically important. Key to this approach is targeting highly conserved antigenic epitopes to reduce the risk of vaccine escape in heterologous tick populations.

methodsWe evaluated amino acid conservation within 14 tick proteins across 167 R. microplus collected from geographically diverse locations in the Americas and Pakistan using polymerase chain reaction (PCR) amplicon sequencing and in silico translation of exons.

resultsWe found that amino acid conservation varied considerably across these proteins. Only the voltage-dependent anion channel (VDAC) was fully conserved in all R. microplus samples (protein similarity 1.0). Four other proteins were highly conserved: the aquaporin RmAQP1 (0.989), vitellogenin receptor (0.985), serpin-1 (0.985), and subolesin (0.981). In contrast, the glycoprotein Bm86 was one of the least conserved (0.889). The Bm86 sequence used in the original Australian TickGARD vaccine carried many amino acid replacements compared with the R. microplus populations examined here, supporting the hypothesis that this vaccine target is not optimal for use in the Americas. By mapping amino acid replacements onto predicted three-dimensional (3D) protein models, we also identified amino acid changes within several small-peptide vaccines targeting portions of the aquaporin RmAQP2, chitinase, and Bm86.

conclusionsThese findings emphasize the importance of thoroughly analyzing protein variation within anti-tick vaccine targets across diverse tick populations before selecting candidate vaccine antigens. When considering protein conservation alone, RmAQP1, vitellogenin receptor, serpin-1, subolesin, and especially VDAC rank as high-priority anti-tick vaccine candidates for use in the Americas and perhaps globally.

Indexed as

Arthropod ProteinsCattle DiseasesRhipicephalusTick InfestationsVaccinesAmericasAmino Acid SequenceAnimalsBabesiosisCattleConserved SequenceEpitopesPakistanArthropod ProteinsEpitopesVaccinesAnti-tick vaccineConserved targetsR. annulatusRhipicephalus microplusSurface-exposed epitopes

Identifiers

PMID40234925
PMCPMC12001435

What Socratic holds

Textmetadata
LicenceCC BY
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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.