The B Subunit of PirAB vp  Toxin Secreted from  Vibrio parahaemolyticus  Causing AHPND Is an Amino Sugar Specific Lectin

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Abstract

Vibrio parahaemolyticus ( Vp) is the etiological agent of the acute hepatopancreatic necrosis disease (AHPND) in Penaeus vannamei shrimp. Vp possesses a 63–70 kb conjugative plasmid that encodes the binary toxin PirA ^vp /PirB ^vp . The 250 kDa PirAB ^vp complex was purified by affinity chromatography with galactose-sepharose 4B and on a stroma from glutaraldehyde-fixed rat erythrocytes column, as a heterotetramer of PirA ^vp and PirB ^vp subunits. In addition, recombinant pirB (rPirB ^vp ) and pirA (rPirA ^vp ) were obtained. The homogeneity of the purified protein was determined by SDS-PAGE analysis, and the yield of protein was 488 ng/100 μg of total protein of extracellular products. The PirAB ^vp complex and the rPirB ^vp showed hemagglutinating activity toward rat erythrocytes. The rPirA ^vp showed no hemagglutinating capacity toward the animal red cells tested. Among different mono and disaccharides tested, only GalNH ₂ and GlcNH ₂ were able to inhibit hemagglutination of the PirAB ^vp complex and the rPirB ^vp . Glycoproteins showed inhibitory specificity, and fetuin was the glycoprotein that showed the highest inhibition. Other glycoproteins, such as mucin, and glycosaminoglycans, such as heparin, also inhibited the activity. Desialylation of erythrocytes enhanced the hemagglutinating activity. This confirms that Gal or Gal (β1,4) GlcNAc are the main ligands for PirAB ^vp . The agglutinating activity of the PirAB ^vp complex and the rPirB ^vp is not dependent on cations, because addition of Mg ²⁺ or Ca ²⁺ showed no effect on the protein capacity. Our results strongly suggest that the PirB ^vp subunit is a lectin, which is part of the PirA/PirB ^vp complex, and it seems to participate in bacterial pathogenicity.

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Demystifying heparan sulfate-protein interactions.

Ding Xu, Jeffrey Esko (2014)

Numerous proteins, including cytokines and chemokines, enzymes and enzyme inhibitors, extracellular matrix proteins, and membrane receptors, bind heparin. Although they are traditionally classified as heparin-binding proteins, under normal physiological conditions these proteins actually interact with the heparan sulfate chains of one or more membrane or extracellular proteoglycans. Thus, they are more appropriately classified as heparan sulfate-binding proteins (HSBPs). This review provides an overview of the various modes of interaction between heparan sulfate and HSBPs, emphasizing biochemical and structural insights that improve our understanding of the many biological functions of heparan sulfate.

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Determination of the infectious nature of the agent of acute hepatopancreatic necrosis syndrome affecting penaeid shrimp.

Loc Tran, Linda Nunan, Rita M Redman … (2013)

A new emerging disease in shrimp, first reported in 2009, was initially named early mortality syndrome (EMS). In 2011, a more descriptive name for the acute phase of the disease was proposed as acute hepatopancreatic necrosis syndrome (AHPNS). Affecting both Pacific white shrimp Penaeus vannamei and black tiger shrimp P. monodon, the disease has caused significant losses in Southeast Asian shrimp farms. AHPNS was first classified as idiopathic because no specific causative agent had been identified. However, in early 2013, the Aquaculture Pathology Laboratory at the University of Arizona was able to isolate the causative agent of AHPNS in pure culture. Immersion challenge tests were employed for infectivity studies, which induced 100% mortality with typical AHPNS pathology to experimental shrimp exposed to the pathogenic agent. Subsequent histological analyses showed that AHPNS lesions were experimentally induced in the laboratory and were identical to those found in AHPNS-infected shrimp samples collected from the endemic areas. Bacterial isolation from the experimentally infected shrimp enabled recovery of the same bacterial colony type found in field samples. In 3 separate immersion tests, using the recovered isolate from the AHPNS-positive shrimp, the same AHPNS pathology was reproduced in experimental shrimp with consistent results. Hence, AHPNS has a bacterial etiology and Koch's Postulates have been satisfied in laboratory challenge studies with the isolate, which has been identified as a member of the Vibrio harveyi clade, most closely related to V. parahemolyticus.

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History of lectins: from hemagglutinins to biological recognition molecules.

Nathan Sharon, Halina Lis (2004)

The occurrence in nature of erythrocyte-agglutinating proteins has been known since the turn of the 19th century. By the 1960s it became apparent that such proteins also agglutinate other types of cells, and that many of them are sugar-specific. These cell-agglutinating and sugar-specific proteins have been named lectins. Although shown to occur widely in plants and to some extent also in invertebrates, very few lectins had been isolated until the early 1970s, and they had attracted little attention. This attitude changed with the demonstration that lectins are extremely useful tools for the investigation of carbohydrates on cell surfaces, in particular of the changes that the latter undergo in malignancy, as well as for the isolation and characterization of glycoproteins. In subsequent years numerous lectins have been isolated from plants as well as from microorganisms and animals, and during the past two decades the structures of hundreds of them have been established. Concurrently, it was shown that lectins function as recognition molecules in cell-molecule and cell-cell interactions in a variety of biological systems. Here we present a brief account of 100-plus years of lectin research and show how these proteins have become the focus of intense interest for biologists and in particular for the glycobiologists among them.

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Journal

Journal ID (nlm-ta): Pathogens

Journal ID (iso-abbrev): Pathogens

Journal ID (publisher-id): pathogens

Title: Pathogens

Publisher: MDPI

ISSN (Electronic): 2076-0817

Publication date (Electronic): 03 March 2020

Publication date Collection: March 2020

Volume: 9

Issue: 3

Electronic Location Identifier: 182

Affiliations

[1 ]Laboratorio de Bacteriología. Centro de Investigación en Alimentación y Desarrollo, A.C. Unidad de Acuacultura y Manejo Ambiental, Av. Sábalo-Cerritos S/N A.P. 711, Mazatlán, Sinaloa 82112, Mexico

[2 ]Laboratorio de Investigación en Biología Molecular e Inmunología, Unidad Académica de Ciencias Químico Biológicas y Farmacéuticas, Universidad Autónoma de Nayarit, Ciudad de la Cultura, Tepic, Nayarit 63190, Mexico

[3 ]Departamento de Bioquímica, Facultad de Medicina, Universidad Nacional Autónoma de México, Circuito Exterior, Ciudad Universitaria, Coyoacan, CDMX 04510, Mexico; ali@ 123456bq.unam.mx (A.P.); ezenteno@ 123456unam.mx (E.Z.)

[4 ]Laboratorio de Biología Molecular, Instituto de Química, Universidad Nacional Autónoma de México, Circuito Exterior, Ciudad Universitaria, Coyoacan, CDMX 04510, Mexico; pcano@ 123456iquimica.unam.mx

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[* ]Correspondence: ssoto@ 123456ciad.mx ; Tel.: +52-669-989-8700

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Marcelo Victorio-De Los Santos https://orcid.org/0000-0002-0261-5573

Sonia Soto-Rodriguez https://orcid.org/0000-0003-0760-4029

Article

Publisher ID: pathogens-09-00182

DOI: 10.3390/pathogens9030182

PMC ID: 7157558

PubMed ID: 32138213

SO-VID: 86e4609e-2392-4d2c-9216-55c6658fd8be

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Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

The B Subunit of PirAB ^vp Toxin Secreted from Vibrio parahaemolyticus Causing AHPND Is an Amino Sugar Specific Lectin

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Most cited references 61

Demystifying heparan sulfate-protein interactions.

Determination of the infectious nature of the agent of acute hepatopancreatic necrosis syndrome affecting penaeid shrimp.

History of lectins: from hemagglutinins to biological recognition molecules.

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