Detection of the lst gene in different serogroups and LOS immunotypes of Neisseria meningitidis

Tsang, R

doi:10.1016/s0378-1097(01)00189-6

Cited by 4 publications

(2 citation statements)

References 10 publications

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“…The inset above Figure 1a shows a proposed structure for the major LOS species at m/z 4087.76 in N. meningitidis 89I that represents a prototypical Neisserial LOS structure [9,[46][47][48]. The detailed lipid A and oligosaccharide structures depicted for the N. meningitidis 89I LOS, an L4 immunotype [49], are based on MS and NMR studies of the conserved Neisserial lipid A [50] and the L4 oligosaccharide [42]. Proposed compositions for all of the major (M-H) -ions and prompt fragments seen in the LOS from N. meningitidis strains 89I and 701 are given in Table 1, consistent with our previous reports on Neisserial LOS [9,10,13].…”

Section: Molecular Weight Profiling Of Intact Losmentioning

confidence: 99%

Analysis of Bacterial Lipooligosaccharides by MALDI-TOF MS with Traveling Wave Ion Mobility

Phillips

John

Jarvis

2016

J. Am. Soc. Mass Spectrom.

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LOS MALDI IMS-MSAbstract. Lipooligosaccharides (LOS) are major microbial virulence factors displayed on the outer membrane of rough-type Gram-negative bacteria. These amphipathic glycolipids are comprised of two domains, a core oligosaccharide linked to a lipid A moiety. Isolated LOS samples are generally heterogeneous mixtures of glycoforms, with structural variability in both domains. Traditionally, the oligosaccharide and lipid A components of LOS have been analyzed separately following mild acid hydrolysis, although important acid-labile moieties can be cleaved. Recently, an improved method was introduced for analysis of intact LOS by MALDI-TOF MS using a thin layer matrix composed of 2,4,6-trihydroxyacetophenone (THAP) and nitrocellulose. In addition to molecular ions, the spectra show in-source Bprompt^fragments arising from regiospecific cleavage between the lipid A and oligosaccharide domains. Here, we demonstrate the use of traveling wave ion mobility spectrometry (TWIMS) for IMS-MS and IMS-MS/MS analyses of intact LOS from Neisseria spp. ionized by MALDI. Using IMS, the singly charged prompt fragments for the oligosaccharide and lipid A domains of LOS were readily separated into resolved ion plumes, permitting the extraction of specific subspectra, which led to increased confidence in assigning compositions and improved detection of less abundant ions. Moreover, IMS separation of precursor ions prior to collision-induced dissociation (CID) generated time-aligned, clean MS/MS spectra devoid of fragments from interfering species. Incorporating IMS into the profiling of intact LOS by MALDI-TOF MS exploits the unique domain structure of the molecule and offers a new means of extracting more detailed information from the analysis.

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Section: Molecular Weight Profiling Of Intact Losmentioning

confidence: 99%

Analysis of Bacterial Lipooligosaccharides by MALDI-TOF MS with Traveling Wave Ion Mobility

Phillips

John

Jarvis

2016

J. Am. Soc. Mass Spectrom.

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“…Meningococcal strains that belong to groups B, C, W-135 and Y can endogenously sialylate their LNT LOS [32]. Group A strains do not have the capacity to synthesize 59-cytidinemonophospho-N-acetylneuraminic acid (CMP-NANA; the donor molecule for sialic acid) and thus cannot endogenously sialylate their LNT LOS [33,34]. However, they can scavenge CMP-NANA from the host to sialylate their LNT LOS.…”

Section: Author Summarymentioning

confidence: 99%

The meningococcal vaccine candidate Neisserial surface protein A (NspA) binds to Factor H and enhances meningococcal resistance to complement

Lewis¹,

Ngampasutadol²,

Wallace³

et al. 2010

Molecular Immunology

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Glycoengineering with neuraminic acid analogs to label lipooligosaccharides and detect native sialyltransferase activity in Gram-negative bacteria

Alvarado Melendez,

de Jong,

Hartman

et al. 2024

Preprint

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Lipooligosaccharides (LOS) are the most abundant cell surface glycoconjugates on the outer membrane of Gram-negative bacteria. They play important roles in host-microbe interactions. Certain Gram-negative pathogenic bacteria cap their LOS with the sialic acid,N-acetylneuraminic acid (Neu5Ac), to mimic host glycans that among others protects these bacteria from recognition by the hosts immune system. This process of molecular mimicry is not fully understood and remains under investigated. To explore the functional role of sialic acid-capped lipooligosaccharides (LOS) at the molecular level, it is important to have tools readily available for the detection and manipulation of both Neu5Ac on glycoconjugates and the involved sialyltransferases, preferably in live bacteria. We and others have shown that the native sialyltransferases of some Gram-negative bacteria can incorporate extracellular unnatural sialic acid nucleotides onto their LOS. We here report on the expanded use of native bacterial sialyltransferases to incorporate neuraminic acids analogs with a reporter group into the LOS of a variety of Gram-negative bacteria. We show that this approach offers a quick strategy to screen bacteria for the expression of functional sialyltransferases and the ability to use exogenous CMP-Neu5Ac to decorate their glycoconjugates. For selected bacteria we also show this strategy complements two other glycoengineering techniques, Metabolic Oligosaccharide Engineering (MOE) and Selective Exo-Enzymatic Labelling (SEEL), and that together they provide tools to modify, label, detect and visualize sialylation of bacterial LOS.

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Detection of the lst gene in different serogroups and LOS immunotypes of Neisseria meningitidis

Cited by 4 publications

References 10 publications

Analysis of Bacterial Lipooligosaccharides by MALDI-TOF MS with Traveling Wave Ion Mobility

Analysis of Bacterial Lipooligosaccharides by MALDI-TOF MS with Traveling Wave Ion Mobility

The meningococcal vaccine candidate Neisserial surface protein A (NspA) binds to Factor H and enhances meningococcal resistance to complement

Glycoengineering with neuraminic acid analogs to label lipooligosaccharides and detect native sialyltransferase activity in Gram-negative bacteria

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