PubMed Health⌕ Search

PubMed · 9595673

The three-for-one model for gram-negative wall growth: a problem and a possible solution.

Abstract

The murein wall in Gram-negative bacteria is so thin that the mechanism of growth is necessarily complicated. From analytical data of murein components, Höltje suggested a model for the growth mechanism that would lead to safe wall enlargement. The model depended on the formation of trimers of peptidoglycan disaccharides linked via their pentapeptides. In the 'three-for-one' model three oligopeptidoglycan chains are linked to each other in the usual linkages between the carboxyl group of D-alanine residues and the epsilon-amino group of diaminopimelic acid residues; these are designated 'tail-to-tail' linkages. This three-chained raft is then linked to the stress-bearing wall via the formation of trimers, defined as three peptide chains linked together by tail-to-tail linkages. Then by autolyzing the oldest bonds in each trimer, the old chain is excised and the raft becomes part of the stress-bearing wall and the wall is enlarged. There is a problem with the three-for-one model in that it demands a precise fitting of the prefabricated raft of three crosslinked chains to a stress-bearing chain in the wall fabric to allow the series of trimer linkages to form. Because the wall, when bearing stress, must be pulled into a 'honeycomb' structure, the end-to-end distance would be shortened. The possibility is raised here that the glycan chains in the stress-bearing wall are stretched to a sufficient degree by the cell's turgor pressure to compensate for its zig-zag structure; this could allow the model to function. A calculation is presented that assumes that the area of the pores in the fabric, called tessera, is maximized by the cell's turgor pressure. In this case the glycan chain must stretch 10% (and the end-to-end distance of peptide strands stretch 28%) so that the end-to-end distance of a glycan chain in the stress-bearing wall and the unstretched nascent wall can be the same and permit indefinite stable growth.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

A L Koch. 1998-05-01. The three-for-one model for gram-negative wall growth: a problem and a possible solution.. https://doi.org/10.1111/j.1574-6968.1998.tb12989.x

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Glycosylation of serum ribonuclease 1 indicates a major endothelial origin and reveals an increase in core fucosylation in pancreatic cancer.

Human pancreatic ribonuclease 1 (RNase 1) is a glycoprotein expressed mainly by the pancreas and also found in endothelial cells. The diagnosis of pancreatic cancer (PaC) remains difficult and therefore the search for sensitive and specific markers is required. Previous studies showed that RNase 1 from human healthy pancreas contained only neutral glycans, whereas RNase 1 from PaC cell lines contained sialylated structures. To determine whether these glycan tumor cell-associated changes were also characteristic of serum RNase 1 and could be used as a marker of PaC, we have analyzed the glycosylation of serum RNase 1. The origin of serum RNase 1 was also investigated. Serum RNase 1 from two PaC patients and two controls was purified and the glycans analyzed by high-performance liquid chromatography (HPLC)-based sequencing and mass spectrometry. Although normal and tumor serum RNase 1 contained the same glycan structures, there was an increase of 40% in core fucosylation in the main sialylated biantennary glycans in the PaC serum RNase 1. This change in proportion would be indicative of a subset of tumor-associated glycoforms of RNase 1, which may provide a biomarker for PaC. Two-dimensional electrophoresis of the RNase 1 from several endothelial cell lines, EA.hy926, human umbilical vein endothelial cells (HUVEC), human mammary microvessel endothelial cells (HuMMEC), and human lung microvessel endothelial cells (HuLEC), showed basically the same pattern and was also very similar to that of serum RNase 1. RNase 1 from EA.hy926 was then purified and presented a glycosylation profile very similar to that from serum RNase 1, suggesting that endothelial cells are the main source of this enzyme.

Carbohydrate Sequence↗

Intramolecular interchain reactions in bidesmosidic glycosides, a new insight into carbohydrate rearrangements induced by electrospray ionisation.

Glycoconjugates are a class of complex molecules that are widely distributed in the plant kingdom and in some marine organisms. This class of compounds has a wide range of biological activities such as anti-inflammatory, antimicrobial, antifungal, anticancer, antiulcer, and immunoenhancing actions.1-3 Some of them also show various toxic activities such as cytotoxic, hemolytic, cardiotoxic, and teratogenic. Among these compounds, steroidal and triterpenoid saponins have long been known as components of widely used herbal drugs and pharmaceutical preparations; ginseng, Tribulus terrestris, Quillaja saponaria, and Digitalis ssp. are just a few examples. Thus, identification of saponins in herbal drugs used worldwide is of significance in phytochemical and toxicological quality control studies, and for the production of safe health products. Therefore, there is continuing demand for methods to rapidly identify and characterize these natural products.

Carbohydrate Sequence↗