Lectin binding on surfaces of Frankia strains

As a prerequisite for the formation of symbiotic association the two partners must come in contact at their cell surfaces, where the phenomena of specificity and recognition are believed to take place. Therefore, in the case of actinorhizal symbioses, probing of Frankia cell surfaces was investigated with fluorescein-labelled lectins as specific markers for sugar residues. Eleven Frankia isolates grown in vitro and originating from Alnus and Elaeagnus host-plant specificity groups were tested with lectins of different carbohydrate-binding specificities. The N-acetylglucosamine and sialic acid binding lectin groups were able to bind to cell surfaces of both type-N and type-P strains of the Alnus group but not to any Frankia strains of the Elaeagnus group. Sugar residues recognized by these lectin groups on colonies of Frankia strains of the Alnus group were detected on hyphae, vesicles, and sporangia but not on mature spores. The present lectin binding study demonstrates that the use of lectins as bioprobes can be a valid tool in the awaited species definition in the genus Frankia.

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Sialic acid-binding lectin from bullfrog eggs inhibits human malignant mesothelioma cell growth in vitro and in vivo

PLoS ONE ◽

10.1371/journal.pone.0190653 ◽

2018 ◽

Vol 13 (1) ◽

pp. e0190653 ◽

Cited By ~ 6

Author(s):

Takeo Tatsuta ◽

Toshiyuki Satoh ◽

Shigeki Sugawara ◽

Akiyoshi Hara ◽

Masahiro Hosono

Keyword(s):

Sialic Acid ◽

Cell Growth ◽

Malignant Mesothelioma ◽

Sialic Acid Binding ◽

Mesothelioma Cell ◽

Binding Lectin

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Mutations That Affect the Tropism of DA and GDVII Strains of Theiler's Virus In Vitro Influence Sialic Acid Binding and Pathogenicity

Journal of Virology ◽

10.1128/jvi.76.16.8138-8147.2002 ◽

2002 ◽

Vol 76 (16) ◽

pp. 8138-8147 ◽

Cited By ~ 30

Author(s):

Karima Jnaoui ◽

Muriel Minet ◽

Thomas Michiels

Keyword(s):

Sialic Acid ◽

Demyelinating Disease ◽

Binding Capacity ◽

Single Amino Acid ◽

Sialic Acid Binding ◽

Encephalomyelitis Virus ◽

The Central Nervous System ◽

Different Strains ◽

Single Amino Acid Mutation

ABSTRACT Theiler's murine encephalomyelitis virus (TMEV) is a natural pathogen of the mouse. The different strains of TMEV are divided into two subgroups according to the pathology they provoke. The neurovirulent strains GDVII and FA induce an acute fatal encephalitis, while persistent strains, like DA and BeAn, cause a chronic demyelinating disease associated with viral persistence in the central nervous system. Different receptor usage was proposed to account for most of the phenotype difference between neurovirulent and persistent strains. Persistent but not neurovirulent strains were shown to bind sialic acid. We characterized DA and GDVII derivatives adapted to grow on CHO-K1 cells. Expression of glycosaminoglycans did not influence infection of CHO-K1 cells by parental and adapted viruses. Mutations resulting from adaptation of DA and GDVII to CHO-K1 cells notably mapped to the well-characterized VP1 CD and VP2 EF loops of the capsid. Adaptation of the DA virus to CHO-K1 cells correlated with decreased sialic acid usage for entry. In contrast, adaptation of the GDVII virus to CHO-K1 cells correlated with the appearance of a weak sialic acid usage for entry. The sialic acid binding capacity of the GDVII variant resulted from a single amino acid mutation (VP1-51, Asn→Ser) located out of the sialic acid binding region defined for virus DA. Mutations affecting tropism in vitro and sialic acid binding dramatically affected the persistence and neurovirulence of the viruses.

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Porcine Arterivirus Infection of Alveolar Macrophages Is Mediated by Sialic Acid on the Virus

Journal of Virology ◽

10.1128/jvi.78.15.8094-8101.2004 ◽

2004 ◽

Vol 78 (15) ◽

pp. 8094-8101 ◽

Cited By ~ 116

Author(s):

Peter L. Delputte ◽

Hans J. Nauwynck

Keyword(s):

Sialic Acid ◽

Alveolar Macrophages ◽

Sialic Acids ◽

Respiratory Syndrome Virus ◽

Specific Monoclonal Antibody ◽

Neuraminidase Treatment ◽

Acid Binding Protein ◽

Sialic Acid Binding ◽

High Mannose ◽

Binding Lectin

ABSTRACT Recently, we showed that porcine sialoadhesin (pSn) mediates internalization of the arterivirus porcine reproductive and respiratory syndrome virus (PRRSV) in alveolar macrophages (Vanderheijden et al., J. Virol. 77:8207-8215, 2003). In rodents and humans, sialoadhesin, or Siglec-1, has been described as a macrophage-restricted molecule and to specifically bind sialic acid moieties. In the current study, we investigated whether pSn is a sialic acid binding protein and, whether so, whether this property is important for its function as a PRRSV receptor. Using untreated and neuraminidase-treated sheep erythrocytes, we showed that pSn binds sialic acid. Furthermore, pSn-specific monoclonal antibody 41D3, which blocks PRRSV infection, inhibited this interaction. PRRSV attachment to and infection of porcine alveolar macrophages (PAM) were both shown to be dependent on the presence of sialic acid on the virus: neuraminidase treatment of virus but not of PAM blocked infection and reduced attachment. Enzymatic removal of all N-linked glycans on the virus with N-glycosidase F reduced PRRSV infection, while exclusive removal of nonsialylated N-linked glycans of the high-mannose type with endoglycosidase H had no significant effect. Free sialyllactose and sialic acid containing (neo)glycoproteins reduced infection, while lactose and (neo)glycoproteins devoid of sialic acids had no significant effect. Studies with linkage-specific neuraminidases and lectins indicated that α2-3- and α2-6-linked sialic acids on the virion are important for PRRSV infection of PAM. From these results, we conclude that pSn is a sialic acid binding lectin and that interactions between sialic acid on the PRRS virion and pSn are essential for PRRSV infection of PAM.

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