On the relations between the elemental surface composition of yeasts and bacteria and their charge and hydrophobicity

Mozes, Nava; Léonard, A.; Rouxhet, Paul

doi:10.1016/0005-2736(88)90495-6

Cited by 110 publications

(63 citation statements)

References 24 publications

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“…This agrees with earlier results of Heckels et al, who chemically modified carboxyl and amino groups on whole Gc, found that each modification changed the cell pI, and concluded that both groups contribute to surface charge (23). An ionogenic role for carboxyl groups is contrary to the contention that phosphate groups are the major sources of negative charge on surfaces of intact microorganisms (35). Recent work indicates that marked bacterial cell surface negativity emanates from neuraminic acid moieties on capsules or LOS side chains (2,45) and from sulfate-bearing polymers that may accrete to the bacterial surface (46).…”

Section: Figsupporting

confidence: 92%

Porin polypeptide contributes to surface charge of gonococci

et al. 1997

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Each strain of Neisseria gonorrhoeae elaborates a single porin polypeptide, with the porins expressed by different strains comprising two general classes, Por1A and Por1B. In the outer membrane, each porin molecule folds into 16 membrane-spanning ␤-strands joined by top-and bottom-loop domains. Por1A and Por1B have similar membrane-spanning regions, but the eight surface-exposed top loops (I to VIII) differ in length and sequence. To determine whether porins, and especially their top loop domains, contribute to bacterial cell surface charge, strain MS11 gonococci that were identical except for expressing a recombinant Por1A, Por1B, or mosaic Por1A-1B polypeptide were compared by whole-cell electrophoresis. These porin variants displayed different electrophoretic mobilities that correlated with the net numbers of charged amino acids within surface-exposed loops of their respective porin polypeptides. The susceptibilities of porin variants to polyanionic sulfated polymers correlated roughly with gonococcal surface charge; those porin variants with diminished surface negativity showed increased sensitivity to the polyanionic sulfated compounds. These observations indicate that porin polypeptides in situ contribute to the surface charge of gonococci, and they suggest that the bacterium's interactions with large sulfated compounds are thereby affected.Porin polypeptide is quantitatively prominent in the gonococcal outer membrane (22,27), where it trimerizes and forms water-filled, voltage-regulated, anion-favoring pores that transport charged, hydrophilic atoms and small molecules across the outer membrane (14, 53). Each gonococcal genome contains a single porin gene whose protein product is identical in all variants of a given strain and formerly has been designated major outer membrane protein, principal outer membrane protein, and protein I. Gonococci (Gc) from diverse strains express porin molecules that generally fall into one of two general classes, Por1A and Por1B (5,10,20); these were initially differentiated by their molecular weight, protease susceptibility, and reactivity with monoclonal antibodies (3,16,30). The primary sequences of Por1A and Por1B porin polypeptides are nearly identical in their membrane-spanning regions but are quite different in surface-exposed domains, as predicted (47) and largely confirmed by antibody epitope mapping (5,18,32,49).Several biological attributes of Gc have been correlated with which porin they produce. Por1A organisms predominate among isolates from systemic infections (4, 7), are usually more resistant than Por1B bacteria to killing by normal human sera (24), and are less resistant than Por1B cells to several antibiotics (6); these differences have been confirmed with Gc that express recombinant porin polypeptides (8). The molecular bases for the apparent relationships between porin phenotype and biological behaviors are unknown.Gram-negative bacteria generally exhibit a net negative surface charge (25), whose molecular origins are incompletely defined except for caps...

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Section: Figsupporting

confidence: 92%

Porin polypeptide contributes to surface charge of gonococci

et al. 1997

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“…According to Mozes et al, the concentration ratio of (HO−C, C− O−C)/C,C−(H,C) and C−(O,N)/C is a crucial determinant of surface hydrophobicity in bacteria [26]. According to the above authors, an hydrophobicity increases with an increase in the concentrations of group C−(H,C) which is associated with hydrocarbon-like compounds in a cell.…”

Section: Xps Spectroscopymentioning

confidence: 99%

Assignment of functional groups in Gram-positive bacteria

Buszewski¹

2015

J Anal Bioanal Tech

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The chemical composition, molecular structure and physicochemical properties of five Gram-positive bacterial strain: Bacillus cereus, Bacillus subtilis, Sarcina lutea, Staphylococcus aureus, Micococcus luteus were investigated by Fourier transform infrared (FTIR), X-ray photoelectron spectroscopy (XPS), NMR spectroscopy and intact cell matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (IC MALDI TOF MS). An analysis of FTIR spectra as a function of pH revealed the three major types of cell wall functional groups -carboxyl group, amino group and phosphate group. An analysis of XPS spectra was determinate the major surface components of bacterial cell.13 C NMR and IC MALDI TOF MS spectra of six bacterial species were registered. Our findings indicate that chemical and structural differences in the cell composition of Gram-positive bacteria can be detected.The obtained results also demonstrate that the combination of FTIR, XPS and NMR spectroscopy with IC MALDI TOF MS technique yields useful information and complements other biochemical and physical methods of microbial cells characteristics.

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“…The bacterial structures that affect CSH include outermembrane proteins, lipoproteins, phospholipids, LPS and fimbriae (Mozes et al, 1988(Mozes et al, , 1989. Among these components, the contribution of fimbriae to CSH in P. aeruginosa has been investigated extensively.…”

Section: Effect Of P/t On Cshmentioning

confidence: 99%

Effect of subinhibitory concentration of piperacillin/tazobactam on Pseudomonas aeruginosa

Fonseca

Extremina

Sousa

2004

Journal of Medical Microbiology

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Subinhibitory concentrations (sub-MICs) of antibiotics, although not able to kill bacteria, can modify their physico-chemical characteristics and the architecture of their outermost surface and may interfere with some bacterial functions. This study investigated the ability of sub-MIC piperacillin/ tazobactam (P/T) to interfere with the bacterial virulence parameters of adhesiveness, cell-surface hydrophobicity, motility, biofilm formation and sensitivity to oxidative stress. Antimicrobial activity against five Pseudomonas aeruginosa clinical isolates, representative of clonal lineages of 96 strains of nosocomial origin, and six control strains (ATCC 27853, PAO1, AK1, MT1562, PT623, PAO1algC) was evaluated in vitro using the NCCLS microdilution method. The effects of sub-MIC on bacterial adhesion and biofilm formation were studied using a modified microtitre plate assay. The relative cell-surface hydrophobicity of P. aeruginosa strains was determined by measuring their ability to adhere to n-hexadecane. P. aeruginosa that had been exposed overnight to P/T and incubated with P/T in the plate were also screened for their ability to swim using flagella and to twitch and for their sensitivity to oxidative stress. The results obtained showed that the impact of sub-MIC P/T on bacterial characteristics was different for the various strains of P. aeruginosa. There was a change in bacterial morphology and hydrophobicity that could explain a significant decrease in adhesion values in all clinical isolates and controls tested, a decrease in biofilm formation, a significant increase in sensitivity to oxidative stress, a significant decrease in flagellum-mediated swimming and a decrease in type IV fimbriae-mediated twitching. The results obtained indicate that sub-MIC P/T interferes with the pathogenic potential of P. aeruginosa.

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On the relations between the elemental surface composition of yeasts and bacteria and their charge and hydrophobicity

Cited by 110 publications

References 24 publications

Porin polypeptide contributes to surface charge of gonococci

Porin polypeptide contributes to surface charge of gonococci

Assignment of functional groups in Gram-positive bacteria

Effect of subinhibitory concentration of piperacillin/tazobactam on Pseudomonas aeruginosa

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