Plasmodium berghei: Immunologically active proteins on the sporozoite surface

  • Vermeulen A
  • Van Munster J
  • Meuwissen J
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Abstract

With an improved separation procedure for Plasmodium berghei sporozoites, up to 2000 mosquitoes can be processed in 3 to 4 hr. The method is based on density gradient centrifugation in Percoll. The small amount of contaminating microbial material did not noticeably interfere with the radiolabeling of surface proteins of the purified sporozoites. Two labeled proteins, with molecular weights of about 110,000 and 53,000 daltons, respectively, were identified using sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Both proteins reacted specifically with antibodies against salivary gland sporozoites raised in rabbits and in rats. These two proteins were also present on the surface of "immature" sporozoites isolated from mosquitoes 12 days after the infective blood meal. None of these proteins, apparently, is involved in the cross-reactivity of sporogonic stages with blood stages. © 1982.

Author-supplied keywords

  • Antibody
  • Antigens, sporozoite
  • Gel electrophoresis
  • Gradient centrifugation
  • Malaria, rodent
  • Percoll
  • Plasmodium berghei
  • Protein A
  • Protozoa, parasitic
  • Rabbit
  • Rat
  • Solubilization
  • Sporozoite purification
  • Staphylococcus aureus
  • Surface labeling

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Authors

  • A. N. Vermeulen

  • J. C. Van Munster

  • J. H E Th Meuwissen

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