当前位置： SCI文献检索 > Advances in Experimental Medicine and Biology期刊下所有文献 > Molecular mimicry of host structures by lipooligosaccharides of Neisseria meningitidis: characterization of sialylated and nonsialylated lacto-N-neotetraose (Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc) structures in lipooligosaccharides using monoclonal antibod

Molecular mimicry of host structures by lipooligosaccharides of Neisseria meningitidis: characterization of sialylated and nonsialylated lacto-N-neotetraose (Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc) structures in lipooligosaccharides using monoclonal antibod

Abstract：

:Neisseria meningitidis lipooligosaccharides (LOSs) are classified into 12 immunotypes. Most LOSs are heterogeneous in having a few components by SDS-PAGE analysis that differ antigenically and chemically. We have utilized a monoclonal antibody that recognizes lacto-N-neotetraose (LNnT) and the lectin, Maackia amurensis leukoagglutinin (MAL), which is specific for NeuNAcalpha2-3Galbeta1-4GlcNAc trisacchride sequence to characterize the 12 N. meningitidis LOSs. Using the combination of ELISA, SDS-PAGE, Western blotting, and other chemical analyses, we have shown that the LNnT (Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc) sequence was present in the 4.0-kDa LOS components of seven immunotype LOSs seen on SDS-PAGE. Six of the seven LNnT-containing LOSs also bound the MAL lectin indicating that N-acetylneuraminic acid (NeuNAc) was alpha2,3-linked to the LNnT sequence in the LOSs. Sialylation of the terminal Gal of LNnT-containing 4.0-kDa component caused only a slight increase in its apparent MW to 4100 on SDS-PAGE. The one LOS with the LNnT-containing component, but not MAL-binding, was from a Group A N. meningitidis, which does not synthesize CMP-NeuNAc, the substrate needed for LOS sialylation. Thus, it is concluded (1) a common LNnT sequence is present in seven immunotype LOSs in addition to their immunotype epitopes, and (2) NeuNAc is alpha2 --> 3 linked to the terminal Gal of LNnT if a organism synthesizes CMP-NeuNAc such as Groups B and C organisms. The above conclusions are consistent with the published structures of N. meningitidis LOSs. The results also demonstrate that specific carbohydrate-binding lectins and monoclonal antibodies can be used as simple yet effective tools to characterize specific carbohydrate sequences in a bacterial LOS or LPS such as N. meningitidis LOS. It is intriguing that N. meningitidis LOSs mimic certain glycosphingolipids, such as paragloboside (LNnT-ceramide) and sialylparagloboside, and some glycoproteins of the host in having LNnT and N-acetyllactosamine sequences respectively with or without alpha2 --> 3 linked NeuNAc. Epidemiological studies of N. meningitidis suggest that the molecular mimicry of host structures by its LOS plays a role in the pathogenesis of N. meningitidis by helping the organism to evade host immune defenses in man. The molecular mimicry of host structures by LOS or LPS is also found in other human pathogens such as N. gonorrhoeae, Haemophilus ducreyi, H. influenaze, Moraxella catarrhalis, Campylobacter jejuni, and Helicobacter pylori.

journal_name

Adv Exp Med Biol

journal_title

Advances in experimental medicine and biology

authors

Tsai CM

doi

10.1007/978-1-4615-1267-7_35

subject

Has Abstract

pub_date

2001-01-01 00:00:00

pages

525-42

eissn

0065-2598

issn

2214-8019

journal_volume

491

pub_type

杂志文章,评审

在线工具

Molecular mimicry of host structures by lipooligosaccharides of Neisseria meningitidis: characterization of sialylated and nonsialylated lacto-N-neotetraose (Galbeta1-4GlcNAcbeta1-3Galbeta1-4Glc) structures in lipooligosaccharides using monoclonal antibod