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The most abundant cyst wall proteins of Acanthamoeba castellanii are lectins that bind cellulose and localize to distinct structures in developing and mature cyst walls.

08:00 EDT 16th May 2019 | BioPortfolio

Summary of "The most abundant cyst wall proteins of Acanthamoeba castellanii are lectins that bind cellulose and localize to distinct structures in developing and mature cyst walls."

Acanthamoeba castellanii, which causes keratitis and blindness in under-resourced countries, is an emerging pathogen worldwide, because of its association with contact lens use. The wall makes cysts resistant to sterilizing reagents in lens solutions and to antibiotics applied to the eye.

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This article was published in the following journal.

Name: PLoS neglected tropical diseases
ISSN: 1935-2735
Pages: e0007352

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Medical and Biotech [MESH] Definitions

A species of free-living soil amoebae in the family Acanthamoebidae. It can cause ENCEPHALITIS and KERATITIS in humans.

Proteins that share the common characteristic of binding to carbohydrates. Some ANTIBODIES and carbohydrate-metabolizing proteins (ENZYMES) also bind to carbohydrates, however they are not considered lectins. PLANT LECTINS are carbohydrate-binding proteins that have been primarily identified by their hemagglutinating activity (HEMAGGLUTININS). However, a variety of lectins occur in animal species where they serve diverse array of functions through specific carbohydrate recognition.

Cysts formed from epithelial inclusions in the lines of fusion of the embryonic processes which form the jaws. They include nasopalatine or incisive canal cyst, incisive papilla cyst, globulomaxillary cyst, median palatal cyst, median alveolar cyst, median mandibular cyst, and nasoalveolar cyst.

Protein or glycoprotein substances of plant origin that bind to sugar moieties in cell walls or membranes. Some carbohydrate-metabolizing proteins (ENZYMES) from PLANTS also bind to carbohydrates, however they are not considered lectins. Many plant lectins change the physiology of the membrane of BLOOD CELLS to cause agglutination, mitosis, or other biochemical changes. They may play a role in plant defense mechanisms.

A class of animal lectins that bind specifically to beta-galactoside in a calcium-independent manner. Members of this class are distiguished from other lectins by the presence of a conserved carbohydrate recognition domain. The majority of proteins in this class bind to sugar molecules in a sulfhydryl-dependent manner and are often referred to as S-type lectins, however this property is not required for membership in this class.

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