Linked Life Data

3064030

Source:http://linkedlifedata.com/resource/pubmed/id/3064030

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1989-3-9
pubmed:abstractText
To investigate whether soluble Plasmodium falciparum antigens possess endotoxin-like properties, the interaction of Limulus amoebocyte lysate (LAL) with defined soluble antigens from Plasmodium falciparum was studied by various crossed immunoelectrophoretic methods and immunoblotting. The soluble P. falciparum antigens were purified by affinity chromatography using human IgG from malaria-immune adults as ligand. Of eight possible antigens, at least three were affected by LAL, as indicated by disappearance of these antigens in the precipitation pattern, after the reaction with LAL. One of the LAL-reactive antigens is a heat-stable glycoprotein with the presence of both hydrophilic and hydrophobic regions in its structure. This antigen shows a strong reaction with polymyxin B, and antibodies against it have been shown to be inhibitory to the growth of P. falciparum in culture. It is concluded that LAL reacts with several soluble antigens from P. falciparum and it is suggested that these antigens participate in the induction of protective immunity to malaria, and consequently that one or more of the soluble antigens are candidates for a malaria vaccine.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0141-9838
pubmed:author
pubmed:issnType
Print
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
593-606
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Demonstration of soluble Plasmodium falciparum antigens reactive with Limulus amoebocyte lysate and polymyxin B.
pubmed:affiliation
Treponematoses Department, Statens Seruminstitut, Copenhagen, Denmark.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't