The use of cationized ferritin as an ultrastructural stain for the visualization of bacterial surface structures by SEM

1987 ◽  
Vol 23 (2) ◽  
pp. 252
Author(s):  
Jenny Naimark ◽  
Eli Morgenstern ◽  
Edward A. Bayer ◽  
Raphael Lamed
2016 ◽  
Vol 371 (1695) ◽  
pp. 20150292 ◽  
Author(s):  
Hwang-Soo Joo ◽  
Chih-Iung Fu ◽  
Michael Otto

Antimicrobial peptides (AMPs) are a key component of the host's innate immune system, targeting invasive and colonizing bacteria. For successful survival and colonization of the host, bacteria have a series of mechanisms to interfere with AMP activity, and AMP resistance is intimately connected with the virulence potential of bacterial pathogens. In particular, because AMPs are considered as potential novel antimicrobial drugs, it is vital to understand bacterial AMP resistance mechanisms. This review gives a comparative overview of Gram-positive and Gram-negative bacterial strategies of resistance to various AMPs, such as repulsion or sequestration by bacterial surface structures, alteration of membrane charge or fluidity, degradation and removal by efflux pumps. This article is part of the themed issue ‘Evolutionary ecology of arthropod antimicrobial peptides’.


2017 ◽  
Author(s):  
Hanjeong Harvey ◽  
Joseph Bondy-Denomy ◽  
Hélène Marquis ◽  
Kristina M. Sztanko ◽  
Alan R. Davidson ◽  
...  

ABSTRACTBacterial surface structures such as type IV pili are common receptors for phage. Strains of the opportunistic pathogenPseudomonas aeruginosaexpress one of five different major type IV pilin alleles, two of which are glycosylated with either lipopolysaccharide O-antigen units or polymers of D-arabinofuranose. Here we show that both these post-translational modifications protectP. aeruginosafrom a variety of pilus-specific phages. We identified a phage capable of infecting strains expressing both non-glycosylated and glycosylated pilins, and through construction of a chimeric phage, traced this ability to its unique tail proteins. Alteration of pilin sequence, or masking of binding sites by glycosylation, both block phage infection. The energy invested by prokaryotes in glycosylating thousands of pilin subunits is thus explained by the protection against phage predation provided by these common decorations.SIGNIFICANCEPost-translational modification of bacterial and archaeal surface structures such as pili and flagella is widespread, but the function of these decorations is not clear. We propose that predation by bacteriophages that use these structures as receptors selects for strains that mask potential phage binding sites using glycosylation. Phages are of significant interest as alternative treatments for antibiotic-resistant pathogens, but the ways in which phage interact with host receptors are not well understood. We show that specific phage tail proteins allow for infection of strains with glycosylated pili, providing a foundation for the creation of designer phages that can circumvent first-line bacterial defenses.


1985 ◽  
Vol 152 (3) ◽  
pp. 493-499 ◽  
Author(s):  
E. S. Kalter ◽  
F. C. Jaspers ◽  
W. C. van Dijk ◽  
F. P. Nijkamp ◽  
W. de Jong ◽  
...  

2007 ◽  
Vol 71 (4) ◽  
pp. 551-575 ◽  
Author(s):  
Sean-Paul Nuccio ◽  
Andreas J. Bäumler

SUMMARY Many Proteobacteria use the chaperone/usher pathway to assemble proteinaceous filaments on the bacterial surface. These filaments can curl into fimbrial or nonfimbrial surface structures (e.g., a capsule or spore coat). This article reviews the phylogeny of operons belonging to the chaperone/usher assembly class to explore the utility of establishing a scheme for subdividing them into clades of phylogenetically related gene clusters. Based on usher amino acid sequence comparisons, our analysis shows that the chaperone/usher assembly class is subdivided into six major phylogenetic clades, which we have termed α-, β-, γ-, κ-, π-, and σ-fimbriae. Members of each clade share related operon structures and encode fimbrial subunits with similar protein domains. The proposed classification system offers a simple and convenient method for assigning newly discovered chaperone/usher systems to one of the six major phylogenetic groups.


Pathogens ◽  
2021 ◽  
Vol 10 (9) ◽  
pp. 1098
Author(s):  
Alfonso Olaya-Abril ◽  
José A. González-Reyes ◽  
Manuel J. Rodríguez-Ortega

Infections caused by the Gram-positive bacterium Streptococcus pneumoniae have become a major health problem worldwide because of their high morbidity and mortality rates, especially in developing countries. This microorganism colonizes the human upper respiratory tract and becomes pathogenic under certain circumstances, which are not well known. In the interaction with the host, bacterial surface structures and proteins play major roles. To gain knowledge into gradual changes and adaptive mechanisms that this pathogen undergoes from when it enters the host, we mimicked several in vivo situations representing interaction with epithelial and macrophage cells, as well as a condition of presence in blood. Then, we analyzed, in four pneumococcal strains, two major surface structures, the capsule and extracellular vesicles produced by the pneumococci, as well as surface proteins by proteomics, using the “shaving” approach, followed by LC-MS/MS. We found important differences in both surface ultrastructures and proteins among the culture conditions and strains used. Thus, this work provides insights into physiological adaptations of the pneumococcus when it interacts with the host, which may be useful for the design of strategies to combat infections caused by this pathogen.


1981 ◽  
Vol 8 (4) ◽  
pp. 303-338 ◽  
Author(s):  
J. W. Costerton ◽  
R. T. Irvin ◽  
K.-J. Cheng ◽  
I. W. Sutherland

Microbiology ◽  
2014 ◽  
Vol 160 (12) ◽  
pp. 2561-2582 ◽  
Author(s):  
Zoran Jaglic ◽  
Mickaël Desvaux ◽  
Agnes Weiss ◽  
Live L. Nesse ◽  
Rikke L. Meyer ◽  
...  

The ability of bacteria to bind different compounds and to adhere to biotic and abiotic surfaces provides them with a range of advantages, such as colonization of various tissues, internalization, avoidance of an immune response, and survival and persistence in the environment. A variety of bacterial surface structures are involved in this process and these promote bacterial adhesion in a more or less specific manner. In this review, we will focus on those surface adhesins and exopolymers in selected foodborne pathogens that are involved mainly in primary adhesion. Their role in biofilm development will also be considered when appropriate. Both the clinical impact and the implications for food safety of such adhesion will be discussed.


2015 ◽  
Vol 6 (14) ◽  
pp. 2677-2684 ◽  
Author(s):  
Marta Palacios-Cuesta ◽  
Aitziber L. Cortajarena ◽  
Olga García ◽  
Juan Rodríguez-Hernández

This manuscript describes the fabrication of bacterial surface arrays by using photolithographic techniques having in addition some particularly interesting features.


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