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Literature DB >> 6815092

Sialic acid residues mediate Mycoplasma pneumoniae attachment to human and sheep erythrocytes.

Abstract

The adherence of Mycoplasma pneumoniae to human and sheep erythrocytes was directly related to the presence of sialyl residues on the erythrocytes. Competitive binding studies between M. pneumoniae and M. gallisepticum, known to bind to human erythrocytes via glycophorin, further reinforced the role of sialic acid in this recognition event.

Entities: Chemical Species

Mesh：

Substances：
Glycophorins
Sialic Acids

Year: 1982 PMID： 6815092 PMCID： PMC347745 DOI： 10.1128/iai.38.1.389-391.1982

Source DB: PubMed Journal: Infect Immun ISSN： 0019-9567 Impact factor: 3.441

8 in total

1. Adherence of Mycoplasma gallisepticum to human erythrocytes.

Authors: M Banai; I Kahane; S Razin; W Bredt
Journal: Infect Immun Date: 1978-08 Impact factor: 3.441

2. Electron microscopic studies on the attachment of Mycoplasma pneumoniae to guinea pig erythrocytes.

Authors: H Brunner; H Krauss; H Schaar; H G Schiefer
Journal: Infect Immun Date: 1979-06 Impact factor: 3.441

3. Isolation of mutants of Mycoplasma pneumoniae defective in hemadsorption.

Authors: E J Hansen; R M Wilson; J B Baseman
Journal: Infect Immun Date: 1979-03 Impact factor: 3.441

4. Attachment of Mycoplasma pneumoniae to respiratory epithelium.

Authors: D A Powell; P C Hu; M Wilson; A M Collier; J B Baseman
Journal: Infect Immun Date: 1976-03 Impact factor: 3.441

5. Interaction of Mycoplasma gallisepticum with sialyl glycoproteins.

Authors: L R Glasgow; R L Hill
Journal: Infect Immun Date: 1980-11 Impact factor: 3.441

6. Characterization of hemadsorption-negative mutants of Mycoplasma pneumoniae.

Authors: E J Hansen; R M Wilson; W A Clyde; J B Baseman
Journal: Infect Immun Date: 1981-04 Impact factor: 3.441

7. Attachment of mycoplasmas to erythrocytes: a model to study mycoplasma attachment to the epithelium of the host respiratory tract.

Authors: I Kahane; S Pnini; M Banai; J B Baseman; G H Cassell; W Bredt
Journal: Isr J Med Sci Date: 1981-07

8. Surface parasitism by Mycoplasma pneumoniae of respiratory epithelium.

Authors: P C Hu; A M Collier; J B Baseman
Journal: J Exp Med Date: 1977-05-01 Impact factor: 14.307

8 in total

20 in total

10. Infection of mouse lymphoblastoid cell lines with Mycoplasma hyorhinis: complex nature of mycoplasma-host cell interactions.

Authors: G H Butler; E J Stanbridge
Journal: Infect Immun Date: 1983-12 Impact factor: 3.441

Sialic acid residues mediate Mycoplasma pneumoniae attachment to human and sheep erythrocytes.

1. Adherence of Mycoplasma gallisepticum to human erythrocytes.

2. Electron microscopic studies on the attachment of Mycoplasma pneumoniae to guinea pig erythrocytes.

3. Isolation of mutants of Mycoplasma pneumoniae defective in hemadsorption.

4. Attachment of Mycoplasma pneumoniae to respiratory epithelium.

5. Interaction of Mycoplasma gallisepticum with sialyl glycoproteins.

6. Characterization of hemadsorption-negative mutants of Mycoplasma pneumoniae.

7. Attachment of mycoplasmas to erythrocytes: a model to study mycoplasma attachment to the epithelium of the host respiratory tract.

8. Surface parasitism by Mycoplasma pneumoniae of respiratory epithelium.

1. Synthesis and distribution of CARDS toxin during Mycoplasma pneumoniae infection in a murine model.

2. Sialylated Receptor Setting Influences Mycoplasma pneumoniae Attachment and Gliding Motility.

3. Sequence divergency of the cytadhesin gene of Mycoplasma pneumoniae.

4. Complex signatures of natural selection at GYPA.

5. Multigeneric aggregations among oral bacteria: a network of independent cell-to-cell interactions.

6. Sialic acid on avian erythrocytes.

7. Cloning and characterization of a putative cytadhesin gene (mgc1) from Mycoplasma gallisepticum.

Review 8. Mycoplasma pneumoniae and its role as a human pathogen.

9. Absence of Mycoplasma pneumoniae cytadsorption protein P1 in Mycoplasma genitalium and Mycoplasma gallisepticum.

10. Infection of mouse lymphoblastoid cell lines with Mycoplasma hyorhinis: complex nature of mycoplasma-host cell interactions.