Evidence map›Paper›PMID 10024577›Full record

ArticleInfection and immunity1999

Cryptosporidium parvum sporozoite pellicle antigen recognized by a neutralizing monoclonal antibody is a beta-mannosylated glycolipid.

M W Riggs, M R McNeil, L E Perryman, A L Stone, M S Scherman, R M O'Connor

Open access · bronzeAbstract read
In one paragraph

Article in Infection and immunity, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
3.1field-weighted citation impact, top 10% of its field
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

8 citing papers in PubMed, 32 citations in OpenAlex.

  1. Parasites and immunotherapy: with or against?Journal of parasitic diseases : official organ of the Indian Society for Parasitology · 2016
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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

6 authors at 4 institutions in 1 country.

M W RiggsDepartment of Veterinary Science and Microbiology, University of Arizona, Tucson, Arizona 85721, USA. mriggs@u.arizona.edu
M R McNeil
L E Perryman
A L Stone
M S Scherman
R M O'Connor
Colorado State University · USUniversity of Arizona · USNorth Carolina State University · USUniversity of Florida · US

Funding

PROTECTIVE ANTIGENS IN CRYPTOSPORIDIOSISU01AI030223 · NIAID · UNIVERSITY OF ARIZONA · PI STERLING, CHARLES R. · 1990 to 1996
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MEROZOITE MONOCLONAL ANTIBODY CHARACTERIZATION AND IN VITRO C. PARVUM CULTURINGU19AI030223 · NIAID · UNIVERSITY OF ARIZONA · PI PERRYMAN, LANCE E · 1997 to 1998
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NIAID NIH HHS AI 30223
6 · The paper itself

Abstract

The protozoan parasite Cryptosporidium parvum is an important cause of diarrhea in humans, calves, and other mammals worldwide. No approved vaccines or parasite-specific drugs are currently available for the control of cryptosporidiosis. To effectively immunize against C. parvum, identification and characterization of protective antigens are required. We previously identified CPS-500, a conserved, neutralization-sensitive antigen of C. parvum sporozoites and merozoites defined by monoclonal antibody 18.44. In the present study, the biochemical characteristics and subcellular location of CPS-500 were determined. CPS-500 was chloroform extractable and eluted with acetone and methanol in silicic acid chromatography, consistent with being a polar glycolipid. Following chloroform extraction and silicic acid chromatography, CPS-500 was isolated by high-pressure liquid chromatography for glycosyl analysis, which indicated the presence of mannose and inositol. To identify which component of CPS-500 comprised the neutralization-sensitive epitope recognized by 18.44, the ability of the monoclonal antibody to bind CPS-500 treated with proteases, or with alpha- or beta-glycosidases, was determined. Monoclonal antibody 18.44 did not bind antigen treated with beta-D-mannosidase but did bind antigen treated with alpha-D-mannosidase, other alpha- or beta-glycosidases, or a panel of proteases. These data indicated that the target epitope was dependent on terminal beta-D-mannopyranosyl residues. By immunoelectron microscopy, 18.44 binding was localized to the pellicle and an intracytoplasmic tubulovesicular network in sporozoites. Monoclonal antibody 18.44 also bound to antigen deposited and released onto substrate over the course travelled by gliding sporozoites and merozoites. Surface localization, adhesion and release during locomotion, and neutralization sensitivity suggest that CPS-500 may be involved in motility and invasion processes of the infective zoite stages.

Indexed as

AnimalsAntibodies, MonoclonalAntigens, ProtozoanCattleCryptosporidium parvumGlycolipidsMannosidesMiceMice, Inbred BALB CNeutralization TestsAntibodies, MonoclonalAntigens, ProtozoanGlycolipidsMannosides

Identifiers

PMID10024577
PMCPMC96463
OpenAlexW2122367966

What OpenQuestion holds

Texttitle and abstract
Read underepoch 390

Registered trials

None linked

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 OpenQuestion graph.