Cited by 41Parasitic Diseases Research and TreatmentHelminth infection and controlParasites and Host Interactions

Identification of immunoreactive proteins from the dog heartworm (Dirofilaria immitis) differentially recognized by the sera from dogs with patent or occult infections

Oleaga, Ana, Pérez-Sánchez, Ricardo, Pagés, Elaine, Marcos-Atxutegi, Cristina, Simón, Fernando·2009·Molecular and Biochemical Parasitology

Abstract

Heartworm disease caused by Dirofilaria immitis affects canine and feline hosts. Moreover, the parasite can infect humans, causing pulmonary dirofilariosis. Most affected dogs have patent infections with circulating microfilariae in peripheral blood, although infected dogs sometimes develop occult infections characterized by the absence of microfilariae. Microfilaremic infections (mf+) are associated with a predominant Th2-type immune response, whereas a Th1-type response predominates in amicrofilaremic infections (mf-), suggesting a role for this response in the suppression of circulating microfilariae. However, nothing is known about the molecules involved in the immune regulation of these infections. The objective of the present work was to identify the parasite proteins recognized differentially by the immune response of dogs with patent or occult infections, using two-dimensional electrophoresis and mass spectrometry. Nineteen proteins of D. immitis were identified, of which 6 were immunoreactive against serum samples from both mf+ and mf- dogs, while another two groups of 6 and 7 different proteins were differentially recognized by sera from mf+ or mf- dogs, respectively. The results point to the existence of differential antigen recognition in patent and occult infections due to D. immitis. Several proteins that could be involved in the immune regulation of these infections are identified. Additionally, the findings seem to suggest that some antigens of D. immitis, together with Wolbachia antigens, could contribute to the stimulation of the Th1-type response.

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Crossref · 10.1016/j.molbiopara.2009.03.005

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  • Proteomics with mass spectrometry allowed the simultaneous identification of numerous proteins, comprising 39 proteins from D. immitis and 15 from D. repens, many represented by several isoforms.

    “Together with mass spectrometry, proteomics allowed the simultaneous identification of numerous proteins, comprising 39 proteins from D. immitis and 15 from D. repens, many of which were represented by several isoforms (157,158,313).”

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Authors
Oleaga, A., Pérez-Sánchez, R., Pagés, E., Marcos-Atxutegi, C., & Simón, F.
Affiliations
  • Instituto de Recursos Naturales y Agrobiología de Salamanca (ES)
  • University of Puerto Rico, Medical Sciences Campus (PR)
  • Universidad de Salamanca (ES)
Corresponding author
Oleaga, Ana
Venue
Molecular and Biochemical Parasitology
Publisher
Elsevier BV
Published
2009-08
Volume
166
Issue
2
Pages
134-141
ISSN
0166-6851 (ISSN-L)
OpenAlex
W2048802976
Cited by
41
References
50
Citations by year
2026: 1 · 2023: 2 · 2021: 16 · 2018: 4 · 2017: 1 · 2016: 1 · 2015: 1 · 2014: 3 · 2013: 2 · 2012: 1
FWCI
2.29
Type
journal article
Language
en
Open access
closed
Locations
  • Molecular and Biochemical Parasitology (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • Junta de Castilla y León
  • European Regional Development Fund
Topics
  • Health Sciences › Medicine › Infectious Diseases › Parasitic Diseases Research and Treatment
  • Health Sciences › Veterinary › Small Animals › Helminth infection and control
  • Life Sciences › Immunology and Microbiology › Parasitology › Parasites and Host Interactions
Keywords
Dirofilaria immitis, canine heartworm disease, occult infection, patent infection, microfilaremia, immunoreactive proteins, Th1 response, Th2 immune response, immune regulation
MeSH terms
Amino Acid Sequence, Animals, Antibodies, Helminth, Dirofilaria immitis, Dirofilariasis, Dog Diseases, Dogs, Molecular Sequence Data, Electrophoresis, Gel, Two-Dimensional, Helminth Proteins, Sequence Alignment

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