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PubMed1991

An analysis by rotary shadowing of the structure of the mammalian vitreous humor and zonular apparatus.

An electron microscopic analysis of human and bovine vitreous humor after rotary shadowing showed the presence of both collagen fibrils and an extensive loose network of hyaluronan molecules. No interaction between the collagen fibrils and the hyaluronan molecules was observed under the conditions used for rotary shadowing. Periodic "struts" were present on the surface of the collagen fibrils. These struts showed an organization the same as that previously observed for type IX collagen on the surface of collagen fibrils from chicken cartilage and vitreous. However, the knob of the noncollagenous NC4 domain of cartilage type IX collagen was not observed at the ends of the struts in a manner identical to that of chicken vitreous humor. Zonular fibrils were dissected out from bovine eyes and shown by rotary shadowing to contain a beaded fibril which is similar in morphology to the "elastin-associated" microfibrils of many connective tissues. Experiments in which the zonular fibrils were stretched and fixed prior to rotary shadowing showed that the distance between each bead is variable and can be accounted for by the bowing out of overlapping filaments which connect each bead.

Aged↗
PubMedDate not supplied

Localization of fibrillin-1 in the human term placenta.

OBJECTIVE: We determined the level of message for fibrillin-1, a single-stranded glycoprotein found in the elastic microfibrils of the extracellular matrix, in human placenta compared with other adult human tissues and localized the protein in the term human placenta. METHODS: Northern blot analysis using a cDNA specific for fibrillin-1 was used to compare message levels in several adult human tissues and placenta. Immunohistochemical staining, using a monoclonal antibody to human fibrillin-1, was used to visualize the site of fibrillin-1 in term human placenta. RESULTS: Larger amounts of message for fibrillin-1 were present in placenta than in any of the other tissues tested. Staining for fibrillin-1 was present in the villous stroma but not in the basement membranes, trophoblast cells, or in blood vessels of stem, mature intermediate, or terminal villi. CONCLUSIONS: Fibrillin-1 is distributed extensively in the villous stroma of the term human placenta and may contribute elastic properties to the placenta and basal plate required for an active uterus.

Adult↗
PubMed1995

Fibrillin domain folding and calcium binding: significance to Marfan syndrome.

BACKGROUND: Marfan syndrome is a heritable disorder of connective tissue which has been associated with mutations in a gene encoding fibrillin, a 350 kD glycoprotein found in microfibrils. This protein consists of approximately 60 domains, 47 of which have similarity to epidermal growth factor (EGF). The first mutations to be detected were found in two sporadic cases that had identical Arg to Pro changes within one EGF-like domain. Based on sequence features common to 43 of the EGF-like domains, it was proposed that these domains might bind calcium. Through the synthesis and characterization of wild-type and mutated single domain peptides, we examined the structural and calcium-binding properties of an isolated EGF-like domain from fibrillin and the effects of the Arg to Pro sequence change. RESULTS: A peptide corresponding to the thirteenth putative calcium-binding, EGF-like domain of fibrillin (the site of the first detected mutations) was synthesized. This peptide could be easily oxidized and refolded. The structure of this domain was probed using NMR methods, indicating features characteristic of the known structures of EGF-like domains. The domain bound to calcium with moderate affinity (Kd = 0.6 +/- 0.1 mM) with no major changes in structure induced upon calcium binding. A synthetic peptide containing the Arg to Pro mutation was found to be drastically impaired in its ability to fold in vitro. CONCLUSIONS: As predicted, a fibrillin domain forms a calcium-binding, EGF-like module. As the putative calcium-binding sites are found at the amino-terminal end of the modules, we propose that calcium ions may bind in the interfaces between domains, affecting the overall structure of the protein. The Arg to Pro mutation blocks domain folding in vitro, suggesting that lack of proper domain folding in vivo may contribute to the molecular defects responsible for Marfan syndrome.

Amino Acid Sequence↗
PubMed1996

Analysis of the human gene encoding latent transforming growth factor-beta-binding protein-2.

Transforming growth factor (TGF)-beta is secreted as an inactive complex, which frequently contains a large molecular weight binding protein designated latent TGF-beta-binding protein (LTBP). Recently, the LTBPs have been shown to be a gene family that contains three known members and exhibits a multidomain structure containing cysteine-rich motifs that are also found in the fibrillin gene family. The present work seeks to characterize the gene encoding LTBP-2 and to compare its features to that of the other LTBPs and to the fibrillins. Human fibroblast libraries were used to isolate cDNA encoding LTBP-2 which was then used to identify LTBP-2 transcripts and to isolate the corresponding LTBP-2 gene. The cloned cDNA encodes a 195 kDa protein containing 20 epidermal growth factor (EGF)-like repeats, three repeats containing eight cysteines, and one segment that appears to be a hybrid of the two. Single exons encode EGF repeats while the eight-cysteine repeats are encoded in two exons. Northern analysis identified two transcripts of 7.5 and 9.0 kb, with the presently analyzed cDNA probably corresponding to the 7.5 transcript. Phylogenetic sequence comparisons demonstrated that LTBP-3 is more similar to LTBP-1 than LTBP-2, while LTBP-2 shows the most similarity to the fibrillins. These analyses suggest that LTBP-1 diverged from LTBP-3, and that LTBP-2 diverged from LTBP-1. Within the fibrillin family, fibrillin-1 is nearest to the LTBPs. While the domain structure of LTBP-2 is similar to that of the other LTBPs, LTBP-2 possesses unique regions that make it the largest member of the LTBP family. LTBP-2 may have dual functions as a member of the TGF-beta latent complex and as a structural component of microfibrils.

Adaptor Proteins, Signal Transducing↗
PubMed2006

Influence of thrombin concentration on the mechanical and morphological properties of cell-seeded fibrin hydrogels.

Fibrin is a biopolymer that has been used in a variety of biomaterial, cell delivery and tissue engineering applications. The enzyme thrombin catalyzes the formation of fibrin microfibrils, which form a three-dimensional mesh in which cells can be directly embedded at the time of gel formation. In this study, fibrin hydrogels containing vascular smooth muscle cells were created using varying concentrations of thrombin. Over 7 days in culture, all gels decreased in volume as the fibrin matrix compacted, and the degree of gel compaction increased as thrombin concentration decreased. The material modulus and ultimate tensile stress of the gels also increased with decreasing thrombin concentration. Addition of thrombin to similar constructs made using collagen Type I did not show an effect on gel compaction or mechanical properties, suggesting that these effects were a result of thrombin's action on fibrin polymerization, and not cellular functions. Cell proliferation in fibrin hydrogels was not significantly affected by thrombin addition. Matrix examination using scanning electron microscopy showed increasing fibrin fiber diameters as thrombin concentration decreased. Confocal microscopic imaging of the actin cytoskeleton showed that cell morphology on two-dimensional substrates of fibrin showed marked changes, with higher thrombin concentrations producing cells with longer cellular projections. However, these morphological changes were not as apparent in cells embedded in three-dimensional (3-D) matrices, in which cells exhibited a similar morphology independent of thrombin concentration. These results relate features of the matrix and cellular components of 3-D fibrin constructs to mechanical properties, and contribute to the understanding of structure-function relationships in cell-seeded, 3-D protein hydrogels.

Animals↗
PubMed2004

Molecular cloning and characterization of a novel gene, EMILIN-5, and its possible involvement in skeletal development.

By analyzing expression profiles of human mesenchymal stem cells incubated in osteogenic supplements, we identified and characterized a novel human cDNA, elastin microfibril interface located protein-5 (EMILIN-5), that is likely to play a significant role in the process of osteogenesis. The deduced EMILIN-5 product consists of 766 amino acids with a cysteine-rich EMI domain at the NH(2) terminus. Western blotting detected EMILIN-5 expression in a variety of osteoblastic cell lines. Immunohistochemistry of mouse embryos 13.5 days post-coitus revealed relatively high levels of EMILIN-5 protein in perichondrium cells of developing limbs. Our findings suggest that the EMILIN-5 gene plays an important role in skeletal development.

3T3 Cells↗
PubMed2004

Abnormal bone collagen morphology and decreased bone strength in growth hormone-deficient rats.

Patients with growth hormone deficiency (GHD) have an increased risk of bone fractures. In these patients, the well-described decrease in bone mineral density (BMD) and content (BMC) may, however, not alone explain the increase in fracture rate. Accordingly, the aim of this study was to evaluate collagen morphology and bone mineralisation in cortical bone as well as bone strength in GHD rats to try to clarify the explanation for the increased fracture rate. The Dw-4 rat was used as a model for GHD. This strain of rats has an autosomal recessive disorder, reducing GH synthesis to approximately 10% and growth rate to approximately 40-50% when compared to normal control rats. Five male Dw-4 rats were examined at age 12 weeks and five healthy Lewis rats served as age-matched controls. The animals were examined for (1) bone mineral status by dual energy X-ray absorptometry (DXA) and ash weight/bone volume, (2) biomechanical properties, (3) serum insulin-like growth factor I (IGF-I) and IGF binding protein 3 (IGFBP-3), and (4) collagen morphology of cortical bone from the right femurs was examined by scanning and transmission electron microscopy. A significant decrease was found in serum IGF-I, IGFBP-3 and biomechanical properties in GHD rats compared to controls (P < 0.009). While DXA-derived BMD was decreased, no significant difference was found in ash weight/bone volume. Electron microscopy showed a significant decrease in the number and a significant increase in the diameter of collagen microfibrils in GHD rats as compared to their controls (P < 0.009). In conclusion, we report for the first time that collagen morphology in bone is markedly altered in rats with isolated GHD. Whether similar conditions are present in GHD patients need further investigations. The changes described, however, may provide a co-explanation for the increased fracture rate in GHD.

Absorptiometry, Photon↗
PubMed2006

Physicochemical characterization of cellulose from perennial ryegrass leaves (Lolium perenne).

In this study, we investigated the physicochemical properties of the cellulosic preparations obtained from both untreated perennial ryegrass leaves and de-juiced leaves. It was found that treatment at 22 degrees C with 18% NaOH and 18% KOH for 2h, and 10% NaOH and 10% KOH for 16 h yielded 28.2%, 28.8%, 22.7%, 23.4%, respectively, of 'cellulose' residue from untreated ryegrass leaves and 35.7%, 36.8%, 32.8% and 34.6%, respectively, from the de-juiced leaves. For each cellulosic fraction, the glucose content was 71.6%, 69.6%, 67.8%, 66.7%, 69.7%, 68.6%, 63.9% and 61.7%, respectively. The structure of the cellulose samples was examined using FTIR and CP/MAS (13)C NMR spectroscopy and X-ray diffraction. The cellulosic preparations were free of bound lignin except for noticeable amounts of residual hemicelluloses (28.4-38.3%), and had intrinsic viscosities between 275.1 and 361.0 mL/g, along with molecular weights from 144,130 to 194,930 g/mol. This study found that the cellulose samples isolated from both de-juiced ryegrass leaves and the untreated leaves had a much lower percent crystallinity (33.0-38.6%) than that from wood-based fibres (60-70%) and had much shorter fibres (0.35-0.49 mm) than those of either cereal straws, bagasse or wood. In addition, a partial disruption of the hydrogen bonds and microfibrils may occur during the de-juicing process by mechanical activity, which results in a decreased cellulose crystallinity and fibre length. These findings are significant in relation to hydrolysing ryegrass cellulose for bio-ethanol production.

Carbon Isotopes↗
PubMedDate not supplied

Micromechanical understanding of the cell-wall structure.

For improving properties of pulp fibres, a better understanding of the relationships between its macroscopic mechanical properties, fibre ultrastructure, and properties of the wood polymers is important. This paper discusses such relations between elastic properties of fibres, their matrix structure and the wood polymer elastic constants. It is argued that an orientation of all of the wood polymers in the direction of the cellulose microfibrils is most likely. The elastic longitudinal modulus of cellulose is well described by the value of 134 GPa dominating the longitudinal fibre properties. In the transverse direction the amorphous polymers play a more important role.

Biomechanical Phenomena↗
PubMedDate not supplied

Helicoidal pattern in secondary cell walls and possible role of xylans in their construction.

The helicoidal organization of secondary cell walls is overviewed from several examples. Both the plywood texture and the occurrence of characteristic defects strongly suggest that the wall ordering is relevant of a cholesteric liquid-crystal assembly that is rapidly and strongly consolidated by lignification. A preferential localization of glucuronoxylans, major matrix components, and in vitro re-association experiments emphasize their preeminent role: (1) during the construction of the composite as directing the cellulose microfibrils in a helicoidal array; (2) during the lignification of the composite as a host structure for lignin precursors.

Cell Wall↗
PubMedDate not supplied

Lignification and tension wood.

Hardwood trees are able to reorient their axes owing to tension wood differentiation. Tension wood is characterised by important ultrastructural modifications, such as the occurrence in a number of species, of an extra secondary wall layer, named gelatinous layer or G-layer, mainly constituted of cellulose microfibrils oriented nearly parallel to the fibre axis. This G-layer appears directly involved in the definition of tension wood mechanical properties. This review gathers the data available in the literature about lignification during tension wood formation. Potential roles for lignin in tension wood formation are inferred from biochemical, anatomical and mechanical studies, from the hypotheses proposed to describe tension wood function and from data coming from new research areas such as functional genomics.

Biomechanical Phenomena↗
PubMed2005

Vavraia lutzomyiae n. sp. (Phylum Microspora) infecting the sandfly Lutzomyia longipalpis (Psychodidae, Phlebotominae), a vector of human visceral leishmaniasis.

Vavraia lutzomyiae (Microsporida; Pleistophoridae) is a new species parasitic in the tropical phlebotomine sandfly, Lutzomyia longipalpis (Diptera, Psychodidae, Phlebotominae), a major vector of Leishmania chagasi in Latin America where human visceral leishmaniasis is endemic. Infected larvae and pupae were parasitized in the abdomen, and some adults were parasitized in Malpighian tubules and midgut. The sporogonial plasmodium divided by multiple divisions into up to 64 uninucleate sporoblasts. These stages were surrounded outside the plasmalemma by a thick, amorphous dense coat and transformed into a merontogenetic sporophorous vesicle within which the sporonts developed into sporoblasts. The mature microsporidian spores were broadly ellipsoidal and measured 6.1+/-0.43 x 3.1+/-0.15 microm. The spore wall consisted of a transparent endospore (approximately 100 nm) and a thin electron dense exospore (approximately 30 nm) with the outer limit slightly undulated. Spores contained a polar filament arranged peripherally in a single layer of eight to nine wide anterior coils (approximately 125 nm diameter), and three to four narrow posterior coils (approximately 70 nm diameter). Transverse sections revealed a concentric layer organization with the internal layer surrounded by numerous (up to 25) longitudinal microfibrils. The angle of tilt of the polar filament was about 65-68 degrees.

Animals↗
PubMed2005

Comparative effects of TGF-beta 1 and TGF-beta 2 on extracellular matrix production, proliferation, migration, and collagen contraction of human Tenon's capsule fibroblasts in pseudoexfoliation and primary open-angle glaucoma.

PURPOSE: To comparatively investigate the effects of TGF-beta(1) and TGF-beta(2) on extracellular matrix production, proliferation, migration, and collagen contraction of cultured human Tenon's capsule fibroblasts derived from patients with pseudoexfoliation (PEX) syndrome, PEX glaucoma, primary open-angle glaucoma (POAG), and cataract. METHODS: Tenon's capsule fibroblasts obtained from four groups of patients were cultured and stimulated with different concentrations (0.1-10 ng ml(-1)) of TGF-beta(1) or TGF-beta(2) for up to 14 days. Cell proliferation was determined with the WST-1 colorimetric assay, cell migration by using the Transwell assay system, and collagen contraction by computerised analysis of three-dimensional collagen lattices and immunohistochemistry for alpha-smooth muscle actin expression. Expression and synthesis of extracellular matrix components (fibronectin, collagen types I and III) was assessed by enzyme-linked immunosorbent assays, by real-time RT-PCR, and by transmission electron microscopy. RESULTS: Both TGF-beta(1) and TGF-beta(2) in pathophysiological concentrations of 0.1-5 ng ml(-1) stimulated cell proliferation, migration, collagen contraction, alpha-smooth muscle actin expression as well as mRNA expression and secretion of fibronectin, collagen type I, and collagen type III by Tenon's fibroblasts derived from all groups of patients. TGF-beta stimulation occurred in a concentration-dependent manner with different peak activities associated with different fibroblast functions. There was some variability among the different groups of patients with an increased response of cells derived from PEX and POAG patients as compared to cataract patients. Although no statistically significant differences were found between both TGF-beta isoforms, TGF-beta(1) had a more pronounced stimulatory effect on expression and synthesis of extracellular matrix components including the production of elastic microfibrils, particularly in cells derived from patients with PEX syndrome/glaucoma. CONCLUSIONS: These findings suggest a significant contribution of TGF-beta(1) in addition to TGF-beta(2) to the conjunctival scarring process following glaucoma filtration surgery. Due to its pronounced fibrogenic potential, TGF-beta(1) may become another focus for targeting drug therapy, particularly in patients with PEX glaucoma.

Aged↗
PubMed2006

magp4 gene may contribute to the diversification of cichlid morphs and their speciation.

Lake Victoria harbors more than 300 species of cichlid fish, which are adapted to a variety of ecological niches with various morphological species-specific features. However, it is believed that these species arose explosively within the last 14,000 years and transcripts among Lake Victoria cichlid species are almost identical in sequence. These data prompted us to develop a DNA chip assay to compare patterns of gene expression among cichlid species. We prepared a DNA chip spotted with 6240 elements derived from cichlid expressed sequence tag (EST) clones and successfully characterized gene expression differences between the cichlid species Haplochromis chilotes and Haplochromis sp. "rockkribensis". We identified 14 transcripts that were differentially expressed between these species at an early developmental stage, 15 days post-fertilization (dpf), and several were further analyzed using quantitative real-time PCR (qPCR). One of these differentially expressed transcripts was a homolog of microfibril-associated glycoprotein 4 (magp4), a putative causative gene for the human inherited disease, Smith-Magenis syndrome (SMS), for which facial defects are among the phenotypic features. Further analysis of magp4 expression showed that magp4 was expressed in the jaw portion of cichlid fry and that expression profiles between Haplochromis chilotes and Haplochromis sp. "rockkribensis" differed during development. These data suggest that the differential expression of a gene associated with human cranial morphogenesis may be involved in the diversification of cichlid jaw morphs.

Animals↗
PubMed2006

Characterization of a chitin synthase cDNA and its increased mRNA level associated with decreased chitin synthesis in Anopheles quadrimaculatus exposed to diflubenzuron.

Chitin synthase (EC 2.4.1.16) is a crucial enzyme responsible for chitin biosynthesis in all chitin-containing organisms. This paper reports a complete cDNA encoding chitin synthase 1 (AqCHS1), change of AqCHS1 mRNA level in response to diflubenzuron exposure, and concentration-dependent effect of diflubenzuron on chitin synthesis in the common malaria mosquito (Anopheles quadrimaculatus). The cDNA consists of 5723 nucleotides, including an open reading frame (ORF) of 4734 nucleotides that encode 1578 amino acid residues and a non-translated region of 989 nucleotides. The deduced amino acid sequence contains all the chitin synthase signature motifs (EDR, QRRRW and SWGTR) and shows 97% identity to that of An. gambiae (AgCHS1, XM_321337). Northern blot and real-time quantitative PCR analyses revealed a significant increase of AqCHS1 mRNA level in the larvae exposed to diflubenzuron at 100 and 500 microg/L. As confirmed by real-time quantitative PCR, AqCHS1 mRNA level was enhanced by 2-fold in the larvae exposed to diflubenzuron at 500 microg/L for 24 h. In contrast, exposures of the larvae to diflubenzuron at 4.0, 20, 100 and 500 microg/L for 48 h resulted in decreases of chitin content by 9.0%, 43%, 58% and 76%, respectively. Significantly increased AqCHS1 mRNA level associated with decreased chitin synthesis may imply possible inhibition of chitin synthase, or abnormal chitin synthase translocation or chitin microfibril assembly conferred by diflubenzuron. Increased AqCHS1 expression due to increased transcription and/or increased mRNA stability may serve as a feedback mechanism to compensate such an effect in the mosquitoes. Further studies are necessary to elucidate the relationship between reduced chitin synthesis and increased expression of AqCHS1 in order to shed new light on trafficking and regulation of chitin biosynthesis in the mosquito affected by diflubenzuron.

Amino Acid Sequence↗
PubMed2004

Molecular structure and interaction of recombinant human type XVI collagen.

Collagen XVI is a minor component of at least two different extracellular fibrillar networks of specialized regions of skin and cartilage. In skin, collagen XVI is integrated into particular fibrillin-rich microfibrils lacking an amorphous elastin core. In cartilage, collagen XVI is a component of small heterotypic D-banded fibrils, mainly occurring in the territorial matrix of chondrocytes. Here, we present the first direct evidence for the molecular structure and functional properties of these fibril-associated collagens with interrupted triple helices (FACIT). We have expressed recombinantly the full-length alpha1 chain of human collagen XVI in HEK 293 EBNA cells in large quantities using an episomal expression system. Secreted full-length recombinant collagen XVI forms stable disulfide-bonded homotrimers and is rapidly proteolytically processed to distinct fragments at specific protease sequence motifs, one resembling an aggrecanase recognition site. Limited trypsin digestion assays and thermal transition curves imply sequential thermal denaturation of individual triple helical domains of this recombinant collagen, similar to authentic collagen XVI. Molecular images of collagen XVI reveal rod-like molecules which harbor multiple sharp kinks attributing a highly flexible structure presumably introduced by non-collagenous (NC) regions. Terminally located cloverleaf-shaped nodules correspond to the large NC NC11 domain of trimeric collagen XVI. The total length of individual trimeric recombinant collagen XVI molecules constitutes about 240 nm as calculated by atomic force and negative staining electron microscopy. Recombinant collagen XVI interacts with fibrillin-1 and with fibronectin indicating multiple molecular interactions in which this ubiquitously expressed and versatile FACIT-collagen can participate. In vitro generated collagen XVI provides an indispensable tool for future determination of its function during supramolecular assembly of matrix aggregates and its role in maintenance, organization and interaction of fibrillar structures.

Amino Acid Sequence↗
PubMed2005

Molecular-scale topographic cues induce the orientation and directional movement of fibroblasts on two-dimensional collagen surfaces.

Collagen fibres within the extracellular matrix lend tensile strength to tissues and form a functional scaffold for cells. Cells can move directionally along the axis of fibrous structures, in a process important in wound healing and cell migration. The precise nature of the structural cues within the collagen fibrils that can direct cell movement are not known. We have investigated the structural features of collagen that are required for directional motility of mouse dermal fibroblasts, by analysing cell movement on two-dimensional collagen surfaces. The surfaces were prepared with aligned fibrils of collagen type I, oriented in a predefined direction. These collagen-coated surfaces were generated with or without the characteristic 67 nm D-periodic banding. Quantitative analysis of cell morphodynamics showed a strong correlation of cell elongation and motional directionality with the orientation of D-periodic collagen microfibrils. Neither directed motility, nor cell body alignment, was observed on aligned collagen lacking D-periodicity, or on D-periodic collagen in the presence of peptide containing an RGD motif. The directional motility of fibroblast cells on aligned collagen type I fibrils cannot be attributed to contact guidance, but requires additional structural information. This allows us to postulate a physiological function for the 67 nm periodicity.

Animals↗
PubMed2006

The anchorless adhesin Eap (extracellular adherence protein) from Staphylococcus aureus selectively recognizes extracellular matrix aggregates but binds promiscuously to monomeric matrix macromolecules.

Besides a number of cell wall-anchored adhesins, the majority of Staphylococcus aureus strains produce anchorless, cell wall-associated proteins, such as Eap (extracellular adherence protein). Eap contains four to six tandem repeat (EAP)-domains. Eap mediates diverse biological functions, including adherence and immunomodulation, thus contributing to S. aureus pathogenesis. Eap binding to host macromolecules is unusually promiscuous and includes matrix or matricellular proteins as well as plasma proteins. The structural basis of this promiscuity is poorly understood. Here, we show that in spite of the preferential location of the binding epitopes within triple helical regions in some collagens there is a striking specificity of Eap binding to different collagen types. Collagen I, but not collagen II, is a binding substrate in monomolecular form. However, collagen I is virtually unrecognized by Eap when incorporated into banded fibrils. By contrast, microfibrils containing collagen VI as well as basement membrane-associated networks containing collagen IV, or aggregates containing fibronectin bound Eap as effectively as the monomeric proteins. Therefore, Eap-binding to extracellular matrix ligands is promiscuous at the molecular level but not indiscriminate with respect to supramolecular structures containing the same macromolecules. In addition, Eap bound to banded fibrils after their partial disintegration by matrix-degrading proteinases, including matrix metalloproteinase 1. Therefore, adherence to matrix suprastructures by S. aureus can be supported by inflammatory reactions.

Bacterial Adhesion↗