Serological evidence of Bartonella henselae infection in healthy people in Catalonia, Spain.

Cat scratch disease (CSD), bacillary angiomatosis, hepatic peliosis and some cases of bacteraemia, endocarditis, and osteomyelitis are directly caused by some species of the genus Bartonella. The purpose of this study was to determine the prevalence of IgG antibodies against Bartonella henselae in healthy people and to identify the epidemiological factors involved. Serum samples from 218 patients were examined by indirect immunofluorescence assay (IFA). Significance levels for univariate statistical analysis were determined by the Mann-Whitney U test, chi2 test and Fisher's exact test. Of 218 patients, 99 were female and 119 male, with a median age of 34.36 years (range 0-91 years). Nineteen (8.7%) reacted with B. henselae antigens. Of all the factors concerning the seroprevalence rate being studied (age, sex, contact with animals, residential area), only age was statistically significant. Our serological data seems to indicate that B. henselae is present in Catalonia and could be transmitted to humans.

Bloodstream infections in adults: importance of healthcare-associated infections.

OBJECTIVE: The objective of this study was to evaluate the characteristics of bloodstream infections occurring among outpatients having recent contact with the health care system compared to hospital and community-acquired infections. METHODS: Prospective observational cohort study of adult patients with bloodstream infections at three teaching hospitals. Bloodstream infection was defined as hospital-acquired if the first positive blood culture was performed more than 48 h after admission. Other bloodstream infections were classified as healthcare-associated or community-acquired. RESULTS: A total of 1157 episodes of bloodstream infections were studied; 581 (50.2%) were community-acquired, 295 (25.5%) were hospital-acquired, and 281 (24.3%) were health care-associated. Of the 281 health care-associated bloodstream infections, 68 (24%) occurred in patients residing in a nursing home, 104 (37%) in patients receiving intravenous therapy, health care at home, chemotherapy or attending dialysis, and 169 (60%) in patients hospitalized during the 90 days before their bloodstream infection (some patients belonged to more than one risk category). The highest prevalence rate of MRSA infections occurred in healthcare-associated infections (5%) (p<0.001). A significantly higher mortality rate was seen in the group with healthcare-associated infections (27.5%) than in community-acquired infections (10.4%) (p<0.001). CONCLUSIONS: Our results confirm that healthcare-associated bloodstream infections show important differences from community-acquired bloodstream infections and suggest that empirical antibiotic therapy should be similar to hospital-acquired bloodstream infections, taking into account the epidemiologic characteristics of each region.

Pancoast's syndrome secondary to lung infection with cutaneous fistulisation caused by Staphylococcus aureus.

Apical bronchial carcinoma is the most common cause of Pancoast's syndrome. Of the many other causes reported, infection is a rare one. A literature review is presented and a case of Pancoast's syndrome, secondary to apical lung pneumonia with bronchocutaneous fistulisation caused by Staphylococcus aureus infection, is reported. Clinical and radiological resolution was achieved after treatment with antibiotics.

Q fever in adults: review of 66 clinical cases.

Sixty-six cases of Q fever in adults, serologically confirmed by indirect immunofluorescence, were studied to analyze the epidemiological, clinical and therapeutic aspects of the disease. Eighty-three percent of the patients were male, and the mean age was 44.7 years. Contact with animals was recorded in 24 patients. The main clinical form of presentation was pneumonia (37 cases); eight patients had hypoxia, and five had respiratory failure. The empirical treatment consisted of macrolides in 36% of cases. Evolution was favorable in all cases.

Primary HIV type-1 infection misdiagnosed as Mediterranean spotted fever.

The case studies of four patients, two men and two women between the ages of 42 and 54 years, are described. They presented to a hospital emergency department during the summer months with acute fever and exanthema. These are the primary symptoms of Mediterranean spotted fever (MSF), an endemic rickettsial disease in the Mediterranean basin that is seen particularly during the summer. The patients were clinically diagnosed as having MSF, but their diagnoses were not confirmed by serological testing. One patient was diagnosed with primary human immunodeficiency virus type 1 infection (HIV-1) 10 days later. The remaining three patients were diagnosed with HIV infection years later, but it is very likely that they also had primary HIV infection when MSF was presumed. When a patient develops sudden onset of fever and a maculopapular rash that is characteristic of MSF, the possibility of primary HIV-1 infection should be considered.

Eleven-year study of recurrent pneumococcal bacteremia.

In order to describe the epidemiology and the clinical and microbiological manifestations of recurrent pneumococcal bacteremia, a long-term study was conducted. Between January 1988 and December 1998, a total of 344 episodes of bacteremia caused by pneumococci was detected in 331 patients. Thirteen (3.9%) of these patients experienced recurrent episodes of pneumococcal bacteremia, and all of them had underlying diseases. In 12 of these patients the recurrence was considered to be a reinfection, and in one patient it was considered to be a relapse. Three patients were found to harbor identical strains in both bacteremic episodes, as determined by pulsed-field techniques. Only hematological neoplasia appeared to be a predisposing factor for recurrent pneumococcal bacteremia.

Lysyl oxidase-like protein from bovine aorta. Isolation and maturation to an active form by bone morphogenetic protein-1.

Recently several cDNAs have been described encoding lysyl oxidase-like proteins. Their deduced amino acid sequences are characterized by a strong similarity in the C-terminal region, corresponding to the lysyl oxidase family catalytic domain, and by marked differences in the N-terminal regions. Different biological functions have been described for lysyl oxidases in addition to their traditionally assumed cross-linking role. To answer the question of whether these different functions are carried out by different lysyl oxidases, purified and active forms of these enzymes are required. At present only the classical form of lysyl oxidase has been purified and characterized. The purpose of this study was to isolate and characterize the lysyl oxidase-like protein. In view of the strong sequence homology with the C-terminal domain of other lysyl oxidases, we chose to purify the protein from bovine aorta using antibodies specific to the N-terminal domain of the proenzyme. We have isolated a 56-kDa protein identified by amino acid sequencing as the bovine lysyl oxidase-like precursor, which is cleaved at the Arg-Arg-Arg sequence at positions 89-91 by a furin-like activity, as revealed after deblocking of the N-terminal residue. The immunopurified protein was largely inactive, but further processing in vitro by bone morphogenetic protein-1 led to an enzyme that was active on elastin and collagen substrates.

Folding and activity of recombinant human procollagen C-proteinase enhancer.

Recombinant human procollagen C-proteinase enhancer (rPCPE) was expressed using a baculovirus system and purified to homogeneity using a three-step procedure including heparin affinity chromatography. Heparin binding was dependent on the C-terminal netrin-like domain. The recombinant protein was found to be active, increasing the activity of procollagen C-proteinase/bone morphogenetic protein-1 on type I procollagen in a manner comparable to the native protein. Enhancing activity was dependent on intact disulfide bonding within the protein. By circular dichroism, the observed secondary structure of rPCPE was consistent with the known three-dimensional structures of proteins containing homologous domains.

Short report: isolation and identification of two spotted fever group rickettsial strains from patients in Catalonia, Spain.

Two rickettsial strains, 16B (previously isolated) and FB1, were isolated from blood from patients with Mediterranean spotted fever in Catalonia, Spain. These are the only 2 human rickettsial isolates of the spotted fever group obtained so far in Spain. These strains were identified by the polymerase chain reaction and sequence analysis of a fragment of the outer membrane protein A (ompA) gene. The partial ompA sequence was found to be 100% identical with that of Rickettsia conorii (Malish 7 strain) for both strains. These results confirm the presence of R. conorii in Catalonia, despite the fact that in a previous study, no R. conorii were isolated, but a new rickettsial strain of the spotted fever group (Bar29) was isolated from dog ticks (Rhipicephalus sanguineus) in Catalonia. Further studies are necessary to get a better knowledge of the epidemiology of rickettsiae in Catalonia.

Structural requirements for fibromodulin binding to collagen and the control of type I collagen fibrillogenesis--critical roles for disulphide bonding and the C-terminal region.

Fibromodulin belongs to the family of small, leucine-rich proteoglycans which have been reported to interact with collagens and to inhibit type I collagen fibrillogenesis. Decorin and fibromodulin exhibit a noticeable degree of sequence similarity. However, as previously reported [Font, B., Eichenberger, D., Rosenberg, L. M. & van der Rest, M. (1996) Matrix Biol. 15, 341-348] the domains of these molecules implicated in the interactions with type XII and type XIV collagens are different, these being the dermatan sulphate/chondroitin sulphate chain for decorin and the core protein for fibromodulin. At the present time the fibromodulin domains implicated in the interactions with fibrillar collagens remain unknown. In experiments reported here, we have sought to identify the structural requirements for fibromodulin interaction with collagen and for the control of type I collagen fibrillogenesis. Circular dichroism spectra and fibrillogenesis inhibition studies show that fibromodulin structure and its collagen fibrillogenesis control function are strictly dependent on the presence of intact disulphide bridge(s). In addition, we show that the binding of fibromodulin (or fibromodulin-derived fragments) to type I collagen is not necessarily correlated with fibrillogenesis inhibition. To isolate fibromodulin domains, the native proteoglycan was submitted to mild proteolysis. We have isolated an alpha-chymotrypsin-resistant fragment which contains the bulk of the N-terminal and central region of the molecule including the leucine-rich repeats 4 and 6 reported for decorin to be involved in type I collagen binding. This fragment does not bind to type I collagen. Using enzymes with different specificities, a number of large fragments of fibromodulin were obtained, suggesting a compact structure for this molecule which is relatively resistant to proteolysis. None of these N-glycosylated fragments were able to bind to type I collagen in co-sedimentation experiments. Taken together these results suggest that fibromodulin-type I collagen interactions leading to fibrillogenesis inhibition require more than one binding domain. One of these domains could be the C-terminal end of the molecule containing the disulphide loop which is absent in the chymotrypsin-resistant fragment.

Characterization of the interactions of type XII collagen with two small proteoglycans from fetal bovine tendon, decorin and fibromodulin.

In addition to the major collagens, such as type I or type II, connective tissues contain a number of less abundant collagens and proteoglycans, whose association contributes to the different properties of the tissues. Type XII and type XIV collagens have been described in soft connective tissues, and type XIV collagen has been shown to interact specifically with decorin through its glycosaminoglycan chain (Font et al., J. Biol. Chem. 268, 25015-25018, 1993). Interactions between these collagens and the small proteoglycans have been characterized further by studying the binding of type XII collagen to decorin by solid phase assays. Our results show a saturable binding of the proteoglycan through its glycosaminoglycan chain to type XII collagen, which does not seem to involve the large non-collagenous NC3 domain of the molecule. This interaction is strongly inhibited by heparin. Furthermore, we report that another small proteoglycan, fibromodulin, isolated from tendon under non-denaturing conditions, is able to bind to type XII collagen. This interaction has been characterized and, unlike that observed with decorin, type XII collagen-fibromodulin interaction seems to take place with the core protein of the proteoglycan. In addition, we report that type XII-type I collagen interactions are not necessarily mediated by decorin as previously suggested.

Predictive factors for invasive disease due to penicillin-resistant Streptococcus pneumoniae: a population-based study.

A prospective population-based study was carried out to determine predictive factors associated with penicillin-resistant pneumococcal invasive disease. A total of 374 patients (250 males and 124 females; mean age, 50.3 +/- 27 years) with invasive pneumococcal infection were admitted to one of the five hospitals in El Vallés County (an industrial area with 800,000 inhabitants in the province of Barcelona, Spain) over a period of 5 years. Of the 374 episodes, 21 (5.6%) were due to highly penicillin-resistant pneumococci and 67 (17.9%) to intermediately penicillin-resistant pneumococci. Multivariate analysis showed a statistically significant association between infection with intermediately penicillin-resistant pneumococci and an age of 0-4 years (odds ratio [OR] = 5.3; 95% confidence interval [CI] = 2.2-12.6), the presence of an immunosuppressive underlying disease (OR = 3.0; 95% CI = 1.5-6.0), and the previous use of beta-lactam antibiotics (OR = 2.1; 95% CI = 1.0-4.5). Infection with highly penicillin-resistant pneumococci was associated only with the previous use of beta-lactam antibiotics (OR = 5.9; 95% 95% CI = 2.2-15.8). Highly resistant strains were of serotypes 6, 9, 14, 15, 19, and 23, of which all but serotypes 9 and 15 are included in the newly formulated conjugated vaccine.