7B). FM4-64 fluorescence, which is taken up by functional presynaptic terminals, was also detected on beads coated with HA-Cbln1 (Supporting Information Fig. S4A). Furthermore,

synapsin I-immunopositive terminals accumulated around HA-Cbln1-coated beads at extrasynaptic sites that lacked endogenous AMPA receptor clusters (Supporting Information Fig. S4B). These results indicate that exogenous Cbln1 is capable of directly inducing the accumulation of functional synaptic vesicles in non cerebellar neurons. To further evaluate the synaptogenic activity of Cbln family proteins that are expressed Staurosporine ic50 outside the cerebellum, we incubated the beads coated with HA-Cbln1, 2 and 4 with hippocampal and cortical neurons. Immunocytochemical analyses of synapsin I showed that HA-Cbln2 but not HA-Cbln4 or HA-CS-Cbln1 accumulated presynaptic terminals

of hippocampal (Fig. 7C) and cortical (Supporting Information Fig. S5) neurons on the beads. As Cbln4 and Cbln1 are coexpressed in certain brain regions, such as the entorhinal cortex and thalamus, Cbln4 may still work as a heteromeric complex with Cbln1 (Miura et al., 2006; Iijima et al., 2007). To test this possibility, HA-Cbln4 and nontagged Cbln1 were HM781-36B supplier coexpressed in HEK293 cells and HA-Cbln4 homomers and HA-Cbln4/Cbln1 heteromers were recovered by biotinylated anti-HA antibody and immobilized on avidin beads. Immunocytochemical analyses showed that, unlike beads coated with HA-Cbln4, beads containing HA-Cbln4/Cbln1 heteromers accumulated presynaptic terminals of hippocampal neurons (Fig. 7C). Together, these results indicate that, of the Cbln family proteins, Cbln1, Cbln2 and Cbln4/Cbln1 heteromers function as presynaptic organizers by associating with NRXs with the splice site 4 insert in various brain regions at least in vitro. Cbln1 is one of the most recently identified bidirectional synaptic organizers in the cerebellum; Cbln1 secreted from cerebellar granule cells indirectly serves as a postsynaptic organizer by binding to its postsynaptic receptor GluD2 expressed in Purkinje cells and directly induces presynaptic differentiation (Matsuda et al., 2010). Rucaparib mw However,

it remained unclear how Cbln1 binds to the presynaptic sites and interacts with other synaptic organizers. In this study, we found that Cbln1 competed with synaptogenesis mediated by NL-NRX and identified NRX1α(S4+) and NRXβs(S4+) as presynaptic receptors for Cbln1. While this manuscript was in preparation, Uemura et al. (2010) also reported the interaction of Cbln1 with NRXs in the cerebellum. We further showed that not only Cbln1, but also its family member Cbln2 but not Cbln4 specifically bound to NRX1β(S4+) even under low Ca2+-concentrations, which was distinct from the interaction between NRXs and NLs or NRXs and LRRTM2. We also characterized in detail the nature of the tripartite complex NRXs/Cbln1/GluD2 as a bidirectional organizer.

The results support the contention that MRB spread originating from repatriates must be considered. When health authorities implemented the recent protective guidelines, the current process was implemented as a compromise, balancing the absolute need

for such a system with the practical and logistical challenges involved.[1] When these guidelines are followed, the identification of an accepting hospital and bed assignment process becomes very complicated for such evacuation/repatriation companies. Alpelisib in vitro Strict application of guidelines will probably delay the return of patients to the home country. The needs of the individual patient, however, at times exceed the capabilities of local facilities, necessitating urgent and/or emergent evacuation.[15] Moreover, patients becoming ill or injured abroad may cause emotional distress to both the patient and the family, especially in case of mass casualty event, and the earliest repatriation is regarded as a priority.[16] Nonetheless, do the needs of an individual patient outweigh the protection of larger segments of society? This question, along with the medical and logistical challenges faced in these considerations, describes the substantial difficulty faced by the medical team when evacuation/repatriation is required. It is also noteworthy

that we observed Sirolimus purchase poor adherence to the French Health Authorities’ directive. Additional investigation of this poor adherence and consideration of more functional guidelines should be pursued. Outside France, previous programs have been developed, such as the “Search and Destroy” policy that has been conducted in North European countries and Ponatinib mouse has demonstrated its efficacy in limiting MRSA spread.[16] To our knowledge, this kind of regulatory measure is specific to France. For instance, the United States does not have current regulations on this topic.

Very recently, the French Ministry of Health defined a procedure of identification/reporting of repatriated patients to health authorities; MAF follows this new procedure.[17] This study is a retrospective review issued from a single medical agency managing a selected French population. Further, patients meeting inclusion criteria during the study period were transported from only 54 countries. The number of cases who were identified as MRB-carriers is limited. Hence we did not attempt to identify independent risk criteria for MRB colonization. Some relevant information such as the origin of patients (French born, other native related, etc.) and any previous hospitalization within 1 year with prior acquisition of MRB are missing. This study is the initial step of a program we aim to establish both in a prospective fashion and from a multicenter perspective. Furthermore, our study design—retrospective with incomplete follow-up—likely underestimates the magnitude of this problem.

41 protein and ECM components. Therefore, a whole-cell binding assay (Fig. 2) was carried out using the wild-type MGAS 6183 strain, the scl1-inactivated isogenic mutant, and the mutant complemented with plasmid pSL230 expressing in trans the Scl1.41 protein (Caswell et al., 2007). All three strains were first transformed with the plasmid pSB027 to generate GFP-expressing cells (Fig. 2a, images at left). The stability of two plasmids pSL230 and pSB027 within the complemented mutant strain was confirmed by isolating total DNA from these cells (Fig. 2d). Fluorescent GAS strains were next tested for binding to ECM-coated glass cover slips (Fig. 2a, images at middle and right columns). More fluorescent wild-type

cells were seen attached to the cover selleck chemical slips coated with cFn and Lm, as compared with scl1 mutant GAS. Furthermore, complementation of the scl1 mutant with pSL230 considerably increased cell binding

to both ECMs. Quantitative analysis by counting the numbers of GAS cells in random fields fully supported visual observations (Fig. 2b). The scl1-inactivated mutant bound 30% and 45% less to cFn and Lm, respectively, compared with the wild-type strain. Importantly, the complementation of the mutant for Scl1.41 expression restored the wild-type levels of binding to both cFn and Lm, indicating that this phenotype was due to the lack of Scl1 expression. Residual cFn binding by the Scl1 Opaganib order mutant could be attributed to the presence of the prtf2 gene in this strain (Caswell et al., 2007) encoding an additional Fn-binding protein, F2 (Jaffe et al., 1996). Similarly, the observed binding of the Scl1-deficient mutant to Lm could be attributed to Lbp and Shr expression; however, the M41-type GAS was not included in the studies that characterized these ECM-binding proteins (Terao et al., 2002; Fisher et al., 2008). Because lbp and shr genes are conserved among GAS strains of various M-types, we used PCR to demonstrate

the presence of both genes in almost M41-type strain MGAS 6183 (Fig. 2c). Altogether, our results demonstrate that Scl1.41 protein is an important surface adhesin that selectively binds to human cFn and Lm and significantly contributes to ECM– GAS interactions. GAS interactions with ECM components have been exhaustively reported in the literature and considerable effort has been directed toward understanding its function in GAS adherence and internalization pertaining to human disease (Cue et al., 2000). The bulk of that work focuses on Fn, although the effect of exogenous cFn on GAS internalization was not specifically investigated. Far less is known about the contribution of Lm to GAS adherence and internalization. Recently, the Lbp of the M1-type strain was shown to facilitate the adherence to and internalization by HEp-2 cells; however, the observed decrease in internalization of the lbp mutant was not statistically significant compared with the wild-type strain (Terao et al., 2002).

41 protein and ECM components. Therefore, a whole-cell binding assay (Fig. 2) was carried out using the wild-type MGAS 6183 strain, the scl1-inactivated isogenic mutant, and the mutant complemented with plasmid pSL230 expressing in trans the Scl1.41 protein (Caswell et al., 2007). All three strains were first transformed with the plasmid pSB027 to generate GFP-expressing cells (Fig. 2a, images at left). The stability of two plasmids pSL230 and pSB027 within the complemented mutant strain was confirmed by isolating total DNA from these cells (Fig. 2d). Fluorescent GAS strains were next tested for binding to ECM-coated glass cover slips (Fig. 2a, images at middle and right columns). More fluorescent wild-type

cells were seen attached to the cover Akt inhibitor slips coated with cFn and Lm, as compared with scl1 mutant GAS. Furthermore, complementation of the scl1 mutant with pSL230 considerably increased cell binding

to both ECMs. Quantitative analysis by counting the numbers of GAS cells in random fields fully supported visual observations (Fig. 2b). The scl1-inactivated mutant bound 30% and 45% less to cFn and Lm, respectively, compared with the wild-type strain. Importantly, the complementation of the mutant for Scl1.41 expression restored the wild-type levels of binding to both cFn and Lm, indicating that this phenotype was due to the lack of Scl1 expression. Residual cFn binding by the Scl1 CHIR 99021 mutant could be attributed to the presence of the prtf2 gene in this strain (Caswell et al., 2007) encoding an additional Fn-binding protein, F2 (Jaffe et al., 1996). Similarly, the observed binding of the Scl1-deficient mutant to Lm could be attributed to Lbp and Shr expression; however, the M41-type GAS was not included in the studies that characterized these ECM-binding proteins (Terao et al., 2002; Fisher et al., 2008). Because lbp and shr genes are conserved among GAS strains of various M-types, we used PCR to demonstrate

the presence of both genes in Rebamipide M41-type strain MGAS 6183 (Fig. 2c). Altogether, our results demonstrate that Scl1.41 protein is an important surface adhesin that selectively binds to human cFn and Lm and significantly contributes to ECM– GAS interactions. GAS interactions with ECM components have been exhaustively reported in the literature and considerable effort has been directed toward understanding its function in GAS adherence and internalization pertaining to human disease (Cue et al., 2000). The bulk of that work focuses on Fn, although the effect of exogenous cFn on GAS internalization was not specifically investigated. Far less is known about the contribution of Lm to GAS adherence and internalization. Recently, the Lbp of the M1-type strain was shown to facilitate the adherence to and internalization by HEp-2 cells; however, the observed decrease in internalization of the lbp mutant was not statistically significant compared with the wild-type strain (Terao et al., 2002).

However, we did indicate unreliable estimates in those cases according to the NHAMCS guidelines for statistical analysis. Thirdly, among our HRIPD population,

approximately 15% of visits underwent HIV serology testing in the ED. Because of the nature of this nonlongitudinal multi-year survey study and the lack of availability of HIV test results, it is not known whether these cases represented patients with an initial HIV diagnosis, those with suspected Protein Tyrosine Kinase inhibitor HIV infection, or those for whom HIV testing was performed based on potential occupational or nonoccupational exposure. Inclusion of these patients may accordingly result in overestimation of ED utilization rates for HRIPD patients. Regardless, this group represented a relatively small proportion (15%) of the total number of ED visits included in the study. Lastly, Federal, military, and VA hospitals were not included in the NHAMCS database, which might limit the generalizability of this study. The prevalence of HIV infection in military applicants and VA hospitals has been estimated to range

from 0.01 to 1.85%, whereas the national estimate was 0.32% in 2000 [22–25]. Consequently, we could not extrapolate to draw conclusions as to whether HRIPD visits would be more or less common in military or VA hospitals. Furthermore, no study has described ED utilization by HRIPD visits in these hospitals. As a result, the extent of the impact of this factor on our national PD98059 price estimates remains unknown. In conclusion, this is the first multi-year, nationally representative non-VA hospital survey to investigate the characteristics of HRIPD visits and their utilization of ED resources. Our results demonstrate that HRIPD visits utilized more resources than non-HRIPD visits with regard to length of ED stay, ordering of diagnostic tests, prescription of medications, and the need for a physician (vs. midlevel) provider. Notably, HRIPD

visits were significantly more likely to result in hospitalization. HRIPD visits also showed increases over time in the need for emergent/urgent care, the number of diagnostic tests performed and the need to be seen by an attending physician. Understanding the utilization patterns of HIV-infected patients in EDs may help to guide approaches to preventing overuse of ED and hospital resources, and could be helpful also in optimizing allocation of limited resources for the care of those with HIV/AIDS. Future studies should be directed towards identifying approaches to reduce the need for, and costs associated with, HRIPD visits. “
“HIV and antiretroviral (ART) exposure in utero may have deleterious effects on the infant, but uncertainty still exists. The objective of this study was to evaluate aspects of mitochondrial DNA (mtDNA) content, mitochondrial function and oxidative stress simultaneously in placenta, umbilical cord blood and infant blood in HIV/ART-exposed infants compared with uninfected controls.

brasilense (Thirunavukkarasu et al., 2008; Mishra GSK1120212 solubility dmso et al., 2011). Chemotaxis is the ability bacteria have to sense gradients of compounds and to drive motility toward the most appropriate niche and is an important trait for survival in the rhizosphere and in plant–microbe interactions (Alexandre, 2010). Signal transduction systems enable cells to detect and

adapt to these changes by executing appropriate cellular responses, such as regulation of gene expression or modulation of the swimming pattern. The best characterized signal transduction system is the one regulating the run or tumble swimming bias via chemotaxis in Escherichia coli (Wadhams & Armitage, 2004). This signal transduction system consists of a set of conserved proteins, which includes CheA, CheW, CheY, CheB, and CheR and a set of chemoreceptors known as methyl-accepting proteins that perceive environmental cues. In A. brasilense, energy taxis is dominant (Fig. 1), Ixazomib with responses to most stimuli in this bacterium being triggered

by changes in the electron transport system (Alexandre et al., 2000). Greer-Phillips et al. (2004) identified a novel chemoreceptor-like protein, named Tlp1, which serves as an energy taxis transducer. A tlp1 mutant was shown to be deficient in chemotaxis toward several rapidly oxidizable substrates, to taxis to the terminal electron acceptors oxygen and nitrate, and to redox taxis, suggesting that Tlp1 controls energy taxis in A. brasilense. The tlp1 mutant is also impaired in colonization of plant roots (Greer-Phillips et al., 2004). Stephens et al. (2006) characterized the CheB and CheR components of the chemotaxis-like signal transduction pathway Che1 in A. brasilense. Characterization of cheB, cheR, and cheBR null mutants showed that these genes significantly influence chemotaxis and aerotaxis but are not essential for these behaviors, suggesting that multiple chemotaxis systems

are present and contribute to chemotaxis and aerotaxis in A. brasilense. A further study characterized mutants for genes cheA1 and cheY1, also components of the Che1 system. As for the cheB/cheR mutants, these mutants were defective but not null for chemotaxis and aerotaxis, and showed a minor defect in swimming pattern. Detailed characterizations of these Cetuximab order mutants lead the authors to propose that the Che1 chemotaxis-like pathway modulates cell length as well as flocculation (Bible et al., 2008). Recently, Carreño-López et al. (2009) identified gene chsA as an important component of the chemotaxis signaling pathway in A. brasilense. The encoded protein, ChsA, displays characteristic signaling protein architecture, containing a PAS sensory domain and an EAL domain. The authors showed that a chsA null mutant was impaired in surface motility and chemotactic response, although it was not affected in synthesis of polar and lateral flagella, thus strengthening a key role of this gene in chemotaxis.

, 2007). Rhizobium leguminosarum swarmer cells are resistant to a number of different classes of antibiotics. Similar to the swarming cells of Salmonella (Kim & Surette, 2003) and P. aeruginosa (Lai et al., 2009), this multiresistant phenotype is transient to the swarming state. Reduced permeability of the outer membrane as well as alteration of the cell wall structure might result in decreased effectiveness of antibiotics targeting the cell

wall (Kim et al., 2003; Kim & Surette, 2004). It is believed click here that this reduction in outer membrane permeability may also provide cross-protection against toxins produced by the host as well as other competing bacteria (Kim & Surette, 2004). Similarly, the mechanism responsible for the increased resistance of R. leguminosarum swarmer cells to antibiotics may also provide resistance to antimicrobial compounds produced by the host plant and by other soil bacteria. Because this is the first report on swarming in R. leguminosarum, additional experiments are needed to determine the role of swarming in plant–microorganism interactions. We gratefully acknowledge the support for this work from a Natural Sciences and Engineering Research Council (NSERC) Discovery

Grant to M.F.H. D.D.T. was supported by a Government of Canada graduate scholarship, the Bettina Bahlsen this website scholarship, and the Graeme Bell and Norma Kay Sullivan-Bell Graduate Scholarship in Biology. We thank Rhonda G. Clark and Glen Ong, who constructed the 3841c− strain and the GFP-labeled VF39SM, respectively. We also thank Jan Michiels for valuable information on possible swarming conditions. Fig. S1. Swarming patterns of Rhizobium leguminosarum VF39SM on swarm medium supplemented with 0.1% of the following: (a) glycerol; (b) erythritol; (c) mannitol;

and (d) rhamnose. Video Clip S1. A time-lapse video of Rhizobium leguminosarum VF39SM swarming motility. Please note: Wiley-Blackwell is not Janus kinase (JAK) responsible for the content or functionality of any supporting materials supplied by the authors. Any queries (other than missing material) should be directed to the corresponding author for the article. “
“Bacteriocin produced by Lactobacillus curvatus CWBI-B28wt is not completely effective against Listeria monocytogenes in food models. There is evidence suggesting that bacteriocin-degrading proteolytic enzymes produced by the CWBI-B28wt strain and/or present in the food matrix contribute to this rebound of Listeria growth. To limit this problem, we have partially characterized an approximately 10-kb plasmid responsible for bacteriocin production in L. curvatus CWBI-B28wt. This plasmid was transferred by high-voltage electroporation into a less proteolytic, but technologically competent Lactobacillus strain.

Samples (0.25 mL) were incubated at 37 °C with vigorous stirring in Rapamycin supplier 18-mL flasks. For the DCCD control, samples were preincubated with 100 μM DCCD at room temperature for 30 min. The reaction was initiated with 5 mM succinate. After 2 h, each reaction was stopped with 25 mM EDTA, followed by transfer to ice. Samples were transferred to Eppendorf tubes, boiled for 5 min and centrifuged (10 000

×g, 20 min) to remove denatured protein. In the supernatants, the synthesized glucose-6-phosphate was oxidized by 2.5 mM NADP in the presence of 3 U mL−1 of glucose-6-phosphate dehydrogenase (Roche). NADPH formation was monitored using a spectrophotometer at 340 nm. ATP hydrolysis activity was measured by quantifying the amount of phosphate released (Bell & Doisy, 1920). IMVs (0.5 mg mL−1) INCB024360 cell line from M. bovis BCG or M. smegmatis were incubated in 10 mM HEPES-KOH (pH 7.5), 100 mM KCl, 5 mM MgCl2 at 37 °C. For the DCCD control, samples were preincubated with 100 μM DCCD at room temperature for 30 min. The reaction was initiated by 2 mM ATP. After 30 min, the reaction was quenched by the addition of 2.4% (w/v) trichloroacetic

acid and the membranes were pelleted by centrifugation at 20 800 g and 4 °C for 15 min. Activation by methanol: IMVs (0.5 mg mL−1) were incubated with 17% or 25% methanol. ATP hydrolysis was assayed as described earlier. Activation by PMF: IMVs (2.5 mg mL−1) were incubated in the presence of 10 mM succinate to establish a PMF at 37 °C for 10 min. A mixture of malonate and ATP (final concentrations

are, respectively, 50 and 2 mM) was added and the incubation was quenched by the addition of 2.4% (w/v) trichloroacetic acid after 2.5 min. ATP hydrolysis was assayed as described earlier. Activation by trypsin: IMVs (0.5 mg mL−1) were incubated with trypsin at 30 °C for 10 min. Mycobacterium bovis BCG was treated with 90 or 750 U mL−1 of trypsin, while M. smegmatis was treated with 90 U mL−1 of trypsin. The reaction was terminated by the addition of trypsin inhibitor (1.5 mg of inhibitor per 1.0 mg of trypsin). ATP hydrolysis assay was performed as described earlier. Activation by sulfite: IMVs (0.5 mg mL−1) were incubated with 10 mM sodium sulfite. ATP hydrolysis was assayed as described earlier. To investigate the role of mycobacterial ATP synthase, we prepared functionally coupled IMVs from the slow-growing M. bovis BCG. This strain selleck chemical shares >99.9% DNA sequence identity with M. tuberculosis and strongly resembles M. tuberculosis in terms of sensitivity to diarylquinolines (Mattow et al., 2001; Huitric et al., 2007). For comparison, we carried out the same set of experiments with the fast-growing saprophyte M. smegmatis. To cope with the extremely thick cell envelope of M. bovis BCG, we optimized the preparation of IMVs in terms of the time and temperature of cell envelope digestion by lysozyme, number of French Press passages and subsequent centrifugation steps (cf. Materials and methods).

When subjects directed covert search to the right VF with the search array located 5° left, with eye-gaze at 10° left, the left IPS exhibited a strong BOLD response (Fig. 2H).

However, there was only a weak response when the search was directed to the left VF, with the search array being located at 5° right, and the eyes oriented 10° right relative to the head (Fig. 2G). Hence, the left IPS is much stronger activated for covert search to the right, contralateral VF, independent of the eye-gaze orientation, and the array location in screen coordinates. To quantitatively assess the effect of the FOR on the BOLD response, we calculated PXD101 the percentage signal change for the ROIs in the IPS in both hemispheres and for the ROI centred on the right FEF (Fig. 4A and B). These ROIs were defined by comparing eye-centred contralateral to ipsilateral conditions (see ‘Materials and methods’). As mentioned above, the comparison of non-eye-centred contralateral to ipsilateral conditions did not yield any significantly activated voxels. These ROIs were located in the posterior and anterior part of the left IPS, the posterior right IPS and the right FEF www.selleckchem.com/products/Staurosporine.html (Fig. 4A). These ROIs were included

in the fronto-parietal regions that were shown to be activated based on the contrast [sR(fC), sL(fC), sL(fR), sR(fL)] > [‘all control conditions’]. All four ROIs (left pIPS, left aIPS, right pIPS and right FEF) showed a significant main effect of search condition across all sessions, (Table 2). Further, to test our hypothesis that in these four regions the two eye-centred contralateral conditions

elicited a significantly higher activation, Selleckchem Erlotinib independent of eye gaze or array location with respect to the head or body, we applied in each ROI four t-tests comparing each of the two eye-centred contralateral conditions with the two eye-centred ipsilateral conditions. Thus, we compared sL(fC) > sR(fC), sL(fC) > sR(fL), sL(fR) > sR(fC) and sL(fR) > sR(fL) with paired two-tailed t-tests. The left pIPS and aIPS and right FEF always revealed higher activation when the covert search was directed to the contralateral side in eye-centred FOR (Table 2), confirmed by t-tests corrected for multiple comparison with the Bonferroni–Holm method. The right pIPS showed a significant main effect for the four conditions, P = 0.0082 in the one-way anova, and t-tests revealed two conditions where search directed to the contralateral VF elicited a higher response than ipsilateral (Table 2). Thus, it is the array location or search direction in eye-centred FOR that determines the strength of the BOLD signal in the search-related fronto-parietal and visual cortex. Overall, the quantitative analysis summarized in Fig. 4B exhibited the presence of a spatially selective map of the current focus of visuospatial attention in the IPS and right FEF. Objects within these regions are represented in an eye-centred manner.

When subjects directed covert search to the right VF with the search array located 5° left, with eye-gaze at 10° left, the left IPS exhibited a strong BOLD response (Fig. 2H).

However, there was only a weak response when the search was directed to the left VF, with the search array being located at 5° right, and the eyes oriented 10° right relative to the head (Fig. 2G). Hence, the left IPS is much stronger activated for covert search to the right, contralateral VF, independent of the eye-gaze orientation, and the array location in screen coordinates. To quantitatively assess the effect of the FOR on the BOLD response, we calculated PLX-4720 mw the percentage signal change for the ROIs in the IPS in both hemispheres and for the ROI centred on the right FEF (Fig. 4A and B). These ROIs were defined by comparing eye-centred contralateral to ipsilateral conditions (see ‘Materials and methods’). As mentioned above, the comparison of non-eye-centred contralateral to ipsilateral conditions did not yield any significantly activated voxels. These ROIs were located in the posterior and anterior part of the left IPS, the posterior right IPS and the right FEF Adriamycin in vivo (Fig. 4A). These ROIs were included

in the fronto-parietal regions that were shown to be activated based on the contrast [sR(fC), sL(fC), sL(fR), sR(fL)] > [‘all control conditions’]. All four ROIs (left pIPS, left aIPS, right pIPS and right FEF) showed a significant main effect of search condition across all sessions, (Table 2). Further, to test our hypothesis that in these four regions the two eye-centred contralateral conditions

elicited a significantly higher activation, Thalidomide independent of eye gaze or array location with respect to the head or body, we applied in each ROI four t-tests comparing each of the two eye-centred contralateral conditions with the two eye-centred ipsilateral conditions. Thus, we compared sL(fC) > sR(fC), sL(fC) > sR(fL), sL(fR) > sR(fC) and sL(fR) > sR(fL) with paired two-tailed t-tests. The left pIPS and aIPS and right FEF always revealed higher activation when the covert search was directed to the contralateral side in eye-centred FOR (Table 2), confirmed by t-tests corrected for multiple comparison with the Bonferroni–Holm method. The right pIPS showed a significant main effect for the four conditions, P = 0.0082 in the one-way anova, and t-tests revealed two conditions where search directed to the contralateral VF elicited a higher response than ipsilateral (Table 2). Thus, it is the array location or search direction in eye-centred FOR that determines the strength of the BOLD signal in the search-related fronto-parietal and visual cortex. Overall, the quantitative analysis summarized in Fig. 4B exhibited the presence of a spatially selective map of the current focus of visuospatial attention in the IPS and right FEF. Objects within these regions are represented in an eye-centred manner.