Publication Date:
1986-04-04
Description:
A lectin in Giardia lamblia was activated by secretions from the human duodenum, the environment where the parasite lives. Incubation of the secretions with trypsin inhibitors prevented the appearance of lectin activity, implicating proteases as the activating agent. Accordingly, lectin activation was also produced by crystalline trypsin and Pronase; other proteases tested were ineffective. When activated, the lectin agglutinated intestinal cells to which the parasite adheres in vivo. The lectin was most specific to mannose-6-phosphate and apparently was bound to the plasma membrane. Activation of a parasite lectin by a host protease represents a novel mechanism of host-parasite interaction and may contribute to the affinity of Giardia lamblia to the infection site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lev, B -- Ward, H -- Keusch, G T -- Pereira, M E -- P-1-P30-AM 39428-01/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1986 Apr 4;232(4746):71-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3513312" target="_blank"〉PubMed〈/a〉
Keywords:
Agglutination
;
Animals
;
Duodenum/enzymology/parasitology
;
Giardia/*metabolism
;
*Host-Parasite Interactions
;
Humans
;
Intestine, Small/enzymology/*parasitology
;
Lectins/*metabolism
;
Mice
;
Peptide Hydrolases/*metabolism
;
Sheep
;
Species Specificity
;
Trypsin/metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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