Few data are available on the risk of congenital malformation with first trimester exposure to the newer therapies telbivudine (FDA category B) and entecavir (FDA Category C). The Vismodegib outcome of the pregnancy should be reported to the Interferon Pregnancy and Antiretroviral Pregnancy Registries. 6.1.5 As there is no evidence of any adverse effect on maternal or neonatal health if women become pregnant while taking ART active against HBV, treatment should be continued. Grading: 1C For

tenofovir, emtricitabine and lamivudine, APR [49] and the Development of Antiretroviral Therapy Study (DART) have not identified any increased risk in prevalence or any specific pattern of anomaly, even when administered in the first trimester. Hence, when a patient becomes pregnant on an anti-HBV viral agent as part of their HAART (tenofovir, lamivudine or emtricitabine), as for HIV management, HAART should be continued. This is because the potential risk

to the fetus from drug exposure is outweighed by that of a hepatitis flare or liver disease progression if the drug(s) were to be discontinued in addition to HIV virological rebound and risk of MTCT. Because entecavir has activity against HIV, it is not recommended unless given with active HAART in a coinfected patient. Moreover, it has click here been found to have significant carcinogenic potential in animal studies and therefore its use as an antiviral drug for HBV during pregnancy should be avoided. Lamivudine has been extensively used, as has tenofovir and to a lesser extent emtricitabine, for the treatment of HIV mono-infection during pregnancy, and lamivudine and telbivudine have been used in HBV mono-infected pregnant women and all have been found to be safe. There are limited data on adefovir use in pregnancy and it is not recommended. Where it is being used in a woman for management of HBV but who does not require HIV treatment, this should be switched to tenofovir incorporated into her HAART regimen. In the context of coinfection during pregnancy where HAART is indicated, there is unlikely to be a situation where it would

be used instead of tenofovir. There is no Leukotriene-A4 hydrolase evidence of any adverse effect on maternal health if women become pregnant while taking tenofovir, lamivudine or emtricitabine: these drugs are recommended as NRTI choices in national [169] and international guidelines [154]. 6.1.6 In all HAV non-immune HBV coinfected women, HAV vaccine is recommended after the first trimester as per the normal schedule (0 and 6–12 months) unless the CD4 cell count is <300 cells/μL, when an additional dose may be indicated. Grading: 1D Immunization for HAV uses inactivated vaccines. Data for HAV vaccine in pregnancy are limited. Nevertheless, several guidelines indicate that pregnancy is not a contraindication for HAV immunization, including in HBV coinfected pregnant women [170],[171].

We recommend that patients should be entered into clinical trials, if available (GPP). We recommend that first-line treatment of DLBCL in HIV-positive individuals includes chemotherapy regimens used in HIV-negative patients, such as CHOP or infusional see more therapies such as EPOCH. No randomized studies have been published in the era of ART and hence there is no optimal ‘gold-standard therapy’ (level of evidence

1B). We recommend that chemotherapy regimens should be combined with HAART therapy (level of evidence 1B). We recommend the concomitant administration of rituximab (level of evidence IB). Patients with CD4 cell counts <50 cells/μL may require closer surveillance (GPP). Until recently, patients with HIV-associated BL have been treated similarly to HIV-positive patients with DLBCL. However, in a large retrospective study the

survival of patients with BL was very poor when treated with CHOP or M-BACOD (methotrexate with leucovorin, bleomycin, doxorubicin, cyclophosphamide, vincristine, and dexamethasone), despite adjunctive HAART [54]. This was corroborated by the results of a Phase II prospective study involving 74 patients with HIV-NHL and HIV-BL treated with rituximab and the CDE infusional regimen (R-CDE). In multivariate analysis, a diagnosis of HIV-BL was significantly associated with a worse outcome in comparison to HIV-NHL patients [50]. In the HIV-negative setting, BL is a highly curable malignancy if intensive chemotherapy regimens of short duration are combined with CNS-penetrating therapy RG7204 clinical trial [62–64]. In the UK, the most widely used regimen is CODOX-M/IVAC (cyclophosphamide, Edoxaban vincristine, doxorubicin, methotrexate/ifosfamide, etoposide, cytarabine) and the two MRC/NCRI studies (LY6 and LY10) have stratified patients into low-risk and high-risk (Table 4.6). In low-risk disease, patients receive 3 cycles of CODOX-M and those with high-risk disease receive 4 cycles of chemotherapy alternating between CODOX-M and IVAC. Grade

3/4 haematological toxicity is universal with this regimen with a high incidence of neutropenic fever and mucositis. The reported treatment-related death rate is around 8–14% [62,63]. In the LY6 study, the main toxicity was from the use of high-dose methotrexate at a dose of 6.7 g/m2 [63] and thus in the LY10 study, the dose was reduced to 3 g/m2 [62] without compromising outcomes. In the LY10 study, the 2-year PFS and OS for low-risk disease was 85% and 88%, respectively, and for high risk, 49% and 52%, respectively [62]. Two small retrospective studies and one prospective comparative study [65–67] have demonstrated the feasibility of administering more intensive chemotherapy regimens, such as CODOX-M/IVAC [65] and hyperCVAD (cyclophosphamide, vincristine, doxorubicin, dexamethasone, methotrexate, cytarabine) to HIV-positive patients with BL [66].

, 2001). Template plasmids and oligonucleotides used for genetic constructions are listed in Tables 1 and 2, respectively. The sequence of STY1365 was amplified by PCR and the product was purified using the Nucleotide Removal Kit (Qiagen). check details The purified DNA was digested by PstI/EcoRI (Invitrogen) and cloned in the PstI/EcoRI-digested mid-copy-number vector pSU19

(Bartolome et al., 1991) to yield pRP005 plasmid. To generate pRP010, a PCR product of STY1365 was directly cloned in the pCC1™ vector according to the manufacturer’s instructions (CopyControl™ PCR Cloning Kit, Epicentre). The plasmids were confirmed by PCR, restriction endonuclease assays and sequencing (Macrogen Corp., Rockville, MD). Finally, these plasmids were introduced into the corresponding mutant strain by electroporation. Primers for cloning as well as sequencing are described in Table 2. Salmonella Typhi KPT-330 cell line strains carrying lacZY fusions were grown routinely in LB broth and OD600 nm was monitored. β-Galactosidase activity was measured as described previously (Bucarey et al., 2005). β-Galactosidase activity was calculated as follows:

103× (A420 nm−1.75 × A550 nm) mL−1 min−1/A600 nm, and expressed in Miller Units where A is the absorbance units. Each assay was made in duplicate and repeated at least three times. Isolation of total RNA was performed as described HAS1 previously (Rodas et al., 2010). RT-PCR amplification was performed

with 5 μg of DNAse I-treated RNA using Superscript II RT (Invitrogen). Amplification included 35 cycles (94 °C for 30 s, 58 °C for 45 s and 72 °C for 90 s) followed by a 5-min extension at 72 °C to ensure full extension of amplified fragments. Primers used to amplify STY1365 are described in Table 2. Reverse transcription of 16S rRNA was used as a positive control (Bucarey et al., 2005). DNAse-treated RNA that had not been transcribed was used as negative control. Thirty-microliter aliquots were resolved in 1.5% agarose gels, stained with ethidium bromide and visualized under UV source. The STY1365-3xFLAG fusion protein was detected by Western blotting using an anti-FLAG M2 monoclonal antibody (Sigma). Overnight cultures of S. Typhi strain carrying the FLAG epitope was subcultured in 25 mL of LB broth and grown to an OD600 nm of 0.2 at 37 °C with shaking. Cells were collected by centrifugation, and subcellular fractionation of inner- and outer-membrane proteins was performed (Santiviago et al., 2001; Bucarey et al., 2006). Cytoplasmic fraction was obtained according to the protocol described by Ludwig et al. (1995). Protein fractions were concentrated by precipitation with ice-cold trichloroacetic acid (final concentration 10%) and washed with acetone. Proteins were quantified using the Pierce® BCA Protein Assay Kit (Thermo Scientific).

The protein bands A and B were excised manually and in-gel digested, and then analyzed by LC-MS/MS. MS was analyzed with sequest

software. The lowest Xcorr values of the peptide were set to be 1.9 (+1 charge), 2.2 (+2 charge) and 3.75 (+3 charge), respectively, and ΔCn must be larger than 0.08 (Wang & Yuan, 2005). The matched peptides revealed that the protein A was InhA (Fig. 4b) protein B camelysin (Fig. 4c). To further support the results, shotgun analysis of the sporulated crystal cultures confirmed that the protein of InhA was not Protein Tyrosine Kinase inhibitor expressed in the camelysin-deficient strain. Grass et al. (2004) reported that the molecular mass of metalloproteinase camelysin was 21.569 kDa with a putative signal peptide of 27 amino acids from B. cereus. In the present study, the calY gene encoded a protein with a deduced size of 199 amino acids. signalp 3.0 server (http://www.cbs.dtu.dk/services/SignalP/) analysis showed that the deduced sequence contained a signal peptide. The prediction result revealed that the cleavage sites might be 31/32 (AFF-SD) and 29/30 (TFA-FF). clustalx analysis showed that there was a 99% homology of the camelysin protein between B. cereus and B. thuringiensis as well as homology of their calY gene sequence; the Selleck BTK inhibitor homology between

Bacillus anthracis and B. thuringiensis was 95%. The high degree of homology of camelysin suggested that the genesis of B. thuringiensis camelysin had a close relationship with B. cereus

and B. anthracis, and that it was more closely related to B. cereus. This work demonstrated that the global expression Cediranib (AZD2171) patterns of proteins differed between the wild-type and camelysin-deficient strain as determined by SDS-PAGE (Fig. 4a) associated with MS (Fig. 4b and c). Results of SDS-PAGE and LC-MS/MS suggested that there were many differences after knocking out the calY gene. It was obvious that the InhA was not expressed in the camelysin-deficient strain (Fig. 4a), and that the InhA reappeared in the complementation strain KCTFC (Fig. 4a). Previous studies reported that the inhA promoters of B. thuringiensis were a –35 (TTGAAA) and a –10 (TAAAAT) hexamer, which are highly similar to the σA promoter consensus (TTGACA 17-18N TATAAT) (Grandvalet et al., 2001). Our sequencing results showed that the transcriptional start site and ORF of the inhA gene remained intact after displacing the calY gene. Thus, it is suggested that there is a relationship between camelysin and InhA. InhA was synthesized during the stationary phase (Dalhammar & Steiner, 1984). It was suggested that the inhA transcription might depend on the complex regulatory mechanisms that control later growth development in Bacillus species (Grandvalet et al., 2001). It was previously reported that AbrB and SinR acted as repressors to prevent expression of InhA.

The additional M184I mutation was observed in the plasma RNA but not in the proviral DNA, and confers high-level resistance to 3TC. This patient was treated with d4T, abacavir (ABC) and LPV/r combination therapy for 1 year before being changed to a 3TC+TDF+LPV/r regimen because of poor compliance.

Patient 33 had the M46M/I mixed population in the PR gene at the therapy-naïve stage. The plasma viral load was undetectable under HAART in most cases, selleckchem but follow-up analysis of the proviral resistance mutations showed the presence of mutations detected at the therapy-naïve stage without additional mutations, except in the sequence from patient 36. Overall, comparison of resistance mutation patterns in MK-2206 ic50 CD4 cells with plasma RNA data or follow-up data for CD4 cells revealed similar results for the RT and PR genes, with one or two discrepant mutations. The analysis of DNA resistance evolution in all treated patients showed that the proportion of new mutations was 22%

(n=6) (P<0.0001 for the difference from 0), and these included three new key mutations. However, the appearance of new mutations was not correlated with the time elapsed between sample collections. A logistic regression was performed and a P value of 0.34 [unitary odds ratio (OR) 1.03; global OR 3.24] was obtained. All the other covariates (patient characteristics and use of antiretroviral therapy) were found not to influence the incidence rate of new mutations. The comparison of pre-HAART RNA genotyping with post-treatment DNA sequencing gave calculated prevalences of detected Fossariinae mutations of 59 and 78%, respectively. The proportion of detected mutations (19%) in the DNA was significantly higher than in the pre-HAART RNA by the χ2 test

(P<0.0001), with moderately good agreement between the two methods in terms of the number of detected mutations (kappa coefficient 0.56). A kappa coefficient of 0.50 indicated moderately good agreement in terms of predicted drug activity between the pretreatment RNA and pretreatment DNA mutation profiles, and a kappa coefficient of 0.40 indicated only fairly good agreement between the pretreatment RNA and post-treatment DNA mutation profiles, as a result of the accumulation of new mutations. Genotyping for HIV-1 drug resistance mutations is routinely performed on a plasma sample. At present, guidelines do not recommend HIV-1 drug resistance testing on cellular proviral DNA. The proviral compartment archives the various strains, either wild-type or drug-resistant, that arise during infection. The long-term persistence of archived drug-resistant DNA may jeopardize the efficacy of targeted drugs, and represents the ‘resistance potential’ profile of a patient [40]. This is important when switching antiretroviral agents or initiating treatment in patients without available historical data or conserved samples.

This specificity of PmtMtu functionality means that expression of M. tuberculosis glycoproteins will be better achieved by using a related host-like S. coelicolor with a homologous glycosylation

system, rather than by attempting the heterologous expression of the M. tuberculosis glycosylation system. We are grateful to Dr. Y. López-Vidal for the gift of M. tuberculosis H37Rv DNA, to Dr. Antonio Vallecillo for providing M. smegmatis mc2155 cells, to Dr. F. Bigi for providing the bacterial two-hybrid system, and to the Unidad de Biología Molecular of the Instituto de Fisiología Celular-UNAM LGK-974 solubility dmso for DNA sequencing. This work was supported by research grant 103214 from the SEP-CONACyT mixed fund and by a scholarship to L.E.C.-D. from Consejo Nacional de Ciencia y Tecnología (Mexico) to support her PhD studies at the Programa de Doctorado en Ciencias Biomédicas, Universidad Nacional Autónoma de México. “
“In-Q-Tel, Inc., Arlington, Vincristine VA, USA TMG Biosciences, LLC, Incline Village, NV, USA Systematic Entomology Laboratory,

United States Department of Agriculture, Washington, DC, USA We describe here a strain of Yersinia pestis, G1670A, which exhibits a baseline mutation rate elevated 250-fold over wild-type Y. pestis. The responsible mutation, a C to T substitution in the mutS gene, results in the transition of a highly conserved leucine at position 689 to arginine (mutS(L689R)). When the MutSL689R protein of G1670A was expressed in a ΔmutS derivative of Y. pestis strain EV76, mutation rates observed were equivalent to those observed in G1670A, consistent with a causal association between the mutS mutation and the mutator phenotype. The observation of a mutator allele in Yersinia pestis has potential implications for the study of evolution of this and other

especially dangerous pathogens. “
“Université d’Angers, UMR1345, Institut de Recherches en Horticulture et Semences, Beaucouzé Cedex, France Insitut Micalis (UMR 1319/INRA-Agroparistech) INRA, Jouy en Josas Cedex, France The bacterium Erwinia amylovora causes fire blight, an invasive Y-27632 concentration disease that threatens apple trees, pear trees and other plants of the Rosaceae family. Erwinia amylovora pathogenicity relies on a type III secretion system and on a single effector DspA/E. This effector belongs to the widespread AvrE family of effectors whose biological function is unknown. In this manuscript, we performed a bioinformatic analysis of DspA/E- and AvrE-related effectors. Motif search identified nuclear localization signals, peroxisome targeting signals, endoplasmic reticulum membrane retention signals and leucine zipper motifs, but none of these motifs were present in all the AvrE-related effectors analysed. Protein threading analysis, however, predicted a conserved double β-propeller domain in the N-terminal part of all the analysed effector sequences.

, 2006). Although the growth of this strain on anthranilate as a sole carbon source was not fully restored, it formed tiny colonies on the plate. These findings indicated that the andAc gene is essential for the utilization of tryptophan and anthranilate. To clarify the inducer

of the andA operon, we tested the effects of tryptophan and anthranilate on the induction of the Proteasome inhibitor andA operon using a lacZ reporter strain EN80, which carried an insertion of the lacZ gene downstream of the andA promoter region but still maintains the intact andA operon (see Materials and Methods for details). Figure 2a shows that the andA operon was up-regulated by tryptophan and anthranilate, but not by the other compounds tested (phenylalanine, proline, o-phthalate, benzoate, catechol, and tyrosine). To clarify whether tryptophan itself or its metabolite is an inducer of the andA promoter, 17616ΔkynA, an ATCC 17616 mutant lacking tryptophan dioxygenase was constructed. The andA promoter in this mutant did not respond to tryptophan, and the loss of induction by tryptophan was restored by supplying in trans GSK-3 signaling pathway the wild-type kynA gene (Fig. 2b). In the mutant, andA promoter responded

to anthranilate as in the wild-type cell (Fig. 2c). To investigate the roles of AndR and Fur in the expression of the andA operon, the andA promoter activities were measured Fossariinae in andR and fur mutants. The induction of the andA promoter in M9 medium by anthranilate was abolished in the andR mutant (EN80ΔandR; Fig. 3a). The complementation of the andR gene in trans restored the induction by tryptophan, which was qualitatively confirmed in an X-gal containing medium (data not shown). In the fur mutant (EN80Δfur), the andA promoter activity was decreased

to half the wild-type level, and this decrease was restored by supplying the fur gene in trans (Fig. 3b). We also tested the effect of an iron-chelating agent, 2,2′-dipyridyl, on the andA promoter activity. It decreased the andA promoter activity in the wild-type strain to a level comparable to that in EN80Δfur in the absence of it (Fig. 3b). The effect of agent was not observed in EN80Δfur, and the supplying EN80Δfur in trans with the fur gene restored the effect of 2,2′-dipyridyl (Fig. 3b). We next investigated whether the andA induction in the soil environment is under the control of AndR or Fur. The two reporter strains, EN80ΔandR and EN80Δfur, were inoculated into the soil sample, and after the incubation for 3 weeks, the cells were recovered to measure their LacZ activities (Fig. 3c). In good agreement with the results conducted under the M9 laboratory conditions, the andA promoter induction was strongly and moderately dependent on the andR and fur, respectively. The wild-type levels of activity were also restored by supplying in trans the respective intact genes.

, 2006). Although the growth of this strain on anthranilate as a sole carbon source was not fully restored, it formed tiny colonies on the plate. These findings indicated that the andAc gene is essential for the utilization of tryptophan and anthranilate. To clarify the inducer

of the andA operon, we tested the effects of tryptophan and anthranilate on the induction of the Alectinib andA operon using a lacZ reporter strain EN80, which carried an insertion of the lacZ gene downstream of the andA promoter region but still maintains the intact andA operon (see Materials and Methods for details). Figure 2a shows that the andA operon was up-regulated by tryptophan and anthranilate, but not by the other compounds tested (phenylalanine, proline, o-phthalate, benzoate, catechol, and tyrosine). To clarify whether tryptophan itself or its metabolite is an inducer of the andA promoter, 17616ΔkynA, an ATCC 17616 mutant lacking tryptophan dioxygenase was constructed. The andA promoter in this mutant did not respond to tryptophan, and the loss of induction by tryptophan was restored by supplying in trans selleck screening library the wild-type kynA gene (Fig. 2b). In the mutant, andA promoter responded

to anthranilate as in the wild-type cell (Fig. 2c). To investigate the roles of AndR and Fur in the expression of the andA operon, the andA promoter activities were measured Galeterone in andR and fur mutants. The induction of the andA promoter in M9 medium by anthranilate was abolished in the andR mutant (EN80ΔandR; Fig. 3a). The complementation of the andR gene in trans restored the induction by tryptophan, which was qualitatively confirmed in an X-gal containing medium (data not shown). In the fur mutant (EN80Δfur), the andA promoter activity was decreased

to half the wild-type level, and this decrease was restored by supplying the fur gene in trans (Fig. 3b). We also tested the effect of an iron-chelating agent, 2,2′-dipyridyl, on the andA promoter activity. It decreased the andA promoter activity in the wild-type strain to a level comparable to that in EN80Δfur in the absence of it (Fig. 3b). The effect of agent was not observed in EN80Δfur, and the supplying EN80Δfur in trans with the fur gene restored the effect of 2,2′-dipyridyl (Fig. 3b). We next investigated whether the andA induction in the soil environment is under the control of AndR or Fur. The two reporter strains, EN80ΔandR and EN80Δfur, were inoculated into the soil sample, and after the incubation for 3 weeks, the cells were recovered to measure their LacZ activities (Fig. 3c). In good agreement with the results conducted under the M9 laboratory conditions, the andA promoter induction was strongly and moderately dependent on the andR and fur, respectively. The wild-type levels of activity were also restored by supplying in trans the respective intact genes.

the triple therapy arms in their primary efficacy analyses at week 48 [5, 7]. However, longer term analyses showed a slightly higher

risk of low-level viraemia for patients taking DRV/r monotherapy [6, 8]; so far, the patients with low-level viraemia have not developed phenotypic resistance to PIs. More detailed analyses of these trials may help to identify patients find more at the lowest risk of viraemia during monotherapy treatment, who could be most suitable for treatment with DRV/r monotherapy. In the MONOI trial, patients with low-level viraemia at baseline, problems with adherence or higher HIV DNA levels at baseline were more likely to show elevations in HIV RNA up to week 96 [9]. In a similar analysis of the Only-Kaletra-04 (OK-04) trial of lopinavir/ritonavir monotherapy, patients with poor adherence, lower nadir CD4 cell counts and lower baseline haemoglobin levels were

most likely to lose virological suppression over selleck kinase inhibitor 96 weeks of randomized treatment [10]. In other studies of standard triple combinations of antiretroviral treatment, coinfection with hepatitis C virus (HCV) has been a consistent predictor of lower HIV RNA suppression rates [11-15]. This trend has been seen across trials of PIs [12, 13, 15] and nonnucleoside reverse transcriptase inhibitors [11, 14]. Coinfection with HCV may be associated with prior or current injecting drug use, which could affect adherence to study medication. In addition, the efficacy endpoint used in these HIV clinical trials – the time to loss of virological response (TLOVR) – can be difficult to interpret. This endpoint classifies virological failure as any confirmed elevation above

50 copies/mL, occurring at any time during the trial. However, these elevations in HIV RNA may be low level, may not be associated with drug resistance and may occur for short time periods, with subsequent resuppression of HIV RNA by the Verteporfin manufacturer end of the trial. The results of the MONET trial were analysed at the final week 144 time-point, to assess whether there were baseline factors affecting the efficacy in the two treatment arms. In addition, the efficacy data were analysed by a strict intent-to-treat (ITT) (switches not considered failures) endpoint, which classified patients as success or failure depending on their HIV RNA levels at the end of the trial, regardless of transient elevations in HIV RNA at earlier time-points. The MONET trial recruited patients who had HIV RNA levels below 50 copies/mL at screening, while on a stable triple antiretroviral regimen, for at least 24 weeks, and no history of virological failure since first starting antiretrovirals. The trial methodology has been described previously [5]. Briefly, patients were randomized to receive DRV/r 800/100 mg once daily, either as monotherapy (monotherapy arm) or with two investigator-selected NRTIs (triple therapy arm).

Thus, from the present data, it is not clear whether

the cleavage occurs from the N-terminus or the C-terminus. Thus, the present study, together with the reports of Ramakrishnan et al. (2000), indicates selleckchem a possible role of PE_PGRS30 in latency of the Mtb. Insights into the mechanism of growth retardation brought about by PE_PGRS30 and studies using animal models will determine the precise role of this protein in the biology of Mtb, which will aid in the development of more potent vaccines and drugs against the pathogen. The Department of Biotechnology, New Delhi, is acknowledged for financial support. The Council of Scientific and Industrial Research, New Delhi, is acknowledged for research fellowship to V.K.G. The authors sincerely appreciate the technical help provided by Mr S.C.P. Sharma and Dr Gajender Saini at the Advanced Instrumentation Research Facility (AIRF), JNU, New Delhi, for electron microscopy. “
“There has been tremendous growth in biofilm research in the past three decades. This growth has been reflected in development of a wide variety of experimental, clinical, and theoretical techniques fostered by our increased knowledge. Keeping the theoretical developments abreast of the experimental advancements and ensuring that the theoretical results are

disseminated to the experimental and clinical community is a major challenge. This manuscript provides an overview of recent developments in each scientific selleck screening library domain. More importantly, this manuscript aims to identify

L-NAME HCl areas where the theory lags behind the experimental understanding (and vice versa). The major themes of the manuscript derive from discussions and presentations at a recent interdisciplinary workshop that brought together a variety of scientists whose underlying studies focus on biofilm processes. Defining a microbial biofilm can be challenging. It is usually described as a community of microorganisms bound to a surface and to each other, encased in a self-produced exopolymeric substance. Such a microbial lifestyle is common in the environment, water distribution systems, and many human infections, particularly those involving indwelling devices. The establishment of a biofilm has several advantages to the microorganisms. It provides protection from environmental insults, enhances cell-to-cell communication (including quorum sensing) which can foster genetic exchange, and aids persistence by close interaction with a substratum, even in the presence of significant shear forces. Thus, microbial biofilms are complex, significant, and unique communities of great consequence to many facets of modern life.