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PubMed2006

[Parainfluenza virus infections in pediatric patients with acute respiratory infections in Beijing during 2001 - 2003].

OBJECTIVE: To understand the relationship of parainfluenza virus (PIV) and acute respiratory infections in infants and young children in Beijing, occurred in recent years. METHODS: 3141 throat swab/nasopharyngeal aspirate specimens were collected from infants and young children with acute respiratory tract infections in Beijing from Jan 2001 to Dec 2003. All of these 3141 specimens were inoculated into MDCK cells for influenza virus and PIV isolation, since PIV had been isolated in MDCK cells in this laboratory from preliminary studies. Out of 3141 specimens, 702 were inoculated into MDCK as well as Vero cells to compare the sensitivity on virus isolation of these cell lines by micro plate method. Growth of PIV in cell culture were identified by haemoagglutination test and indirect immunofluorescent assay. RESULTS: The PIV positive cases in Vero cells were also positive in MDCK cells, indicating that the sensitivity for PIV isolation in MDCK was equal to Vero cells. Out of these 3141 specimens, 94 (3.0%) were PIV positive, including 35 (35/1191, 2.9%) of PIV1, 11 (11/1191, 0.9%) of PIV3 in upper respiratory tract infections; 15 (15/1634, 0.9%) of PIV1, 24 (24/1634, 1.5%) of PIV3 in lower respiratory tract infections; 3 (3/207, 1.4%) of PIV in asthma; 1 (1/38) of PIV in patients with fever; 5 (5/71) of PIV in others. Data indicated that among upper respiratory tract infections caused by PIV, PIV1 was more commonly seen than PIV3. CONCLUSION: MDCK cells could be used for PIV isolation from clinical samples while PIV was one of the important pathogenic viruses causing acute respiratory tract infections in infants and young children in Beijing for the recente years.

Acute Disease↗
PubMed1990

Survival and disinfection of parainfluenza viruses on environmental surfaces.

Three dilutions of each of three parainfluenza strains were placed on nonabsorptive (stainless steel, laminated plastic, skin) and absorptive (hospital gown, facial tissue, laboratory coat) surfaces to assess persistence of virus recovery at 0, 0.5, 1, 2, 4, 6, 8, and 10 hours. Virus persisted longest on stainless steel. Additionally, the ability to recover virus was enhanced by increasing the initial concentration of virus in the initial inoculum. Drying of the inoculum on surfaces reduced but did not immediately eliminate the ability to recover virus. Cleaning the contaminated surface with a number of commonly available disinfectant or antiseptic agents reduced or eliminated virus with only short exposure times. It is likely that removal of contaminated material by vigorous cleaning was as important as the actual disinfecting substance. In general, all three strains of parainfluenza virus responded similarly. Persistence of all three strains of parainfluenza virus for up to 10 hours on nonabsorptive surfaces and up to 4 hours on absorptive surfaces suggests a need to consider fomites a possible source of transmission of the parainfluenza viruses inside and outside the hospital.

Clothing↗
PubMed1987

Sequence analysis of the matrix protein gene of human parainfluenza virus type 3: extensive sequence homology among paramyxoviruses.

The sequences of the human parainfluenza virus type 3 (PIV3) matrix (M) mRNA [1150 nucleotides exclusive of poly(A)] and predicted M protein (353 amino acids) were determined by sequence analysis of cloned cDNA and viral genomic RNA. The gene-end sequence of the M gene differed from the semi-conserved gene-end sequence of the other PIV3 genes by an apparent insertion of eight nucleotides. The PIV3 M protein shared high sequence homology with Sendai virus and moderate homology with measles virus and canine distemper virus. Statistical analysis of the available sequences showed that the M protein was the most highly conserved parainfluenza viral protein.

Amino Acid Sequence↗
PubMed1991

Parainfluenza virus infection damages inhibitory M2 muscarinic receptors on pulmonary parasympathetic nerves in the guinea-pig.

1. The effect of viral infection on the function of neuronal M2 muscarinic autoreceptors in the lungs was studied in anaesthetized guinea-pigs. 2. Guinea-pigs were inoculated intranasally with either parainfluenza type 3 or with a vehicle control. Four days later the animals were anaesthetized, paralysed and artificially ventilated. Pulmonary inflation pressure, tidal volume, blood pressure, and heart rate were recorded. Both vagus nerves were cut and electrical stimulation of the distal portions caused bronchoconstriction (measured as an increase in pulmonary inflation pressure) and bradycardia. 3. In control animals, pilocarpine (1-100 micrograms kg-1, i.v.) attenuated vagally-induced bronchoconstriction by stimulating inhibitory M2 muscarinic receptors on parasympathetic nerves in the lungs. Conversely, blockade of these receptors with the antagonist gallamine (0.1-10 mg kg-1, i.v.) produced a marked potentiation of vagally-induced bronchoconstriction. These results confirm previous findings. 4. In guinea-pigs infected with parainfluenza virus, pilocarpine did not inhibit vagally-induced bronchoconstriction. Furthermore, gallamine did not potentiate vagally-induced bronchoconstriction to the same degree as in uninfected controls. 5. There was no increase in baseline pulmonary inflation pressure in the infected animals over the controls. Receptors on airway smooth muscle were unchanged by viral infection since large doses of pilocarpine caused equivalent bronchoconstriction in both groups of animals. Gallamine inhibited the vagally-induced fall in heart rate equally in both groups of animals indicating that virus-induced changes in M2 receptor function on pulmonary parasympathetic nerves are not part of a generalized decrease in M2 receptor function. 6. These results demonstrate that the M2 muscarinic receptor-mediated inhibition of acetylcholine release from parasympathetic nerves in the lungs is decreased in animals infected with parainfluenza virus. Loss of this inhibition would result in increased release of acetylcholine from the parasympathetic nerves and may explain virus-induced airway hyperresponsiveness.

Acetylcholine↗
PubMed2004

Mucosal immunisation of African green monkeys (Cercopithecus aethiops) with an attenuated parainfluenza virus expressing the SARS coronavirus spike protein for the prevention of SARS.

BACKGROUND: The outbreak of severe acute respiratory syndrome (SARS) in 2002 was caused by a previously unknown coronavirus-SARS coronavirus (SARS-CoV). We have developed an experimental SARS vaccine for direct immunisation of the respiratory tract, the major site of SARS- coronavirus transmission and disease. METHODS: We expressed the complete SARS coronavirus envelope spike (S) protein from a recombinant attenuated parainfluenza virus (BHPIV3) that is being developed as a live attenuated, intranasal paediatric vaccine against human parainfluenza virus type 3 (HPIV3). We immunised eight African green monkeys, four with a single dose of BHPIV3/ SARS-S and four with a control, BHPIV3/Ctrl, administered via the respiratory tract. A SARS-coronavirus challenge was given to all monkeys 28 days after immunisation. FINDINGS: Immunisation of animals with BHPIV3/SARS-S induced the production of SARS-coronavirus-neutralising serum antibodies, indicating that a systemic immune response resulted from mucosal immunisation. After challenge with SARS coronavirus, all monkeys in the control group shed SARS coronavirus, with shedding lasting 5-8 days. No viral shedding occurred in the group immunised with BHPIV3/SARS-S. INTERPRETATION: A vectored mucosal vaccine expressing the SARS-coronavirus S protein alone may be highly effective in a single-dose format for the prevention of SARS.

Administration, Intranasal↗
PubMed2000

N-glycosylation contributes to the limited cross-reactivity between hemagglutinin neuraminidase proteins of human parainfluenza virus type 4A and 4B.

cDNAs encoding human parainfluenza virus type 4B (hPIV-4B) hemagglutinin neuraminidase (HN) protein were cloned and the nucleotide sequences were determined. A high degree of identity (81.4%) was observed between the nucleotide sequences of hPIV-4A and -4B HN proteins, and an 87.3% identity was found between the deduced amino acid sequences. This degree of identity is considered to be greater than immunological similarity between hPIV-4A and -4B HN proteins determined using monoclonal antibodies. To elucidate the causes of the antigenic difference between HN proteins of hPIV-4A and -4B, we constructed three cDNAs of hPIV-4B HN whose potential N-glycosylation sites were partially or completely the same as in hPIV-4A HN cDNA. We compared the antigenicity of the expressed wild-type and mutant proteins, and found that the antigenicities of the mutant hPIV-4B HN proteins were more similar to the hPIV-4A HN protein than to the non-mutant hPIV-4B HN protein. This study indicated that the antigenic diversity between hPIV-4A and -4B was partly caused by deletion or creation of glycosylation sites, showing that the point mutations resulting in deletion or creation of glycosylation sites is one of the initial steps leading to the division of virus into subtypes.

Amino Acid Sequence↗
PubMed1996

The role of interleukin-10 in the inhibition of T-cell proliferation and apoptosis mediated by parainfluenza virus type 3.

We have previously demonstrated that parainfluenza virus type 3 (PIV3), a significant respiratory pathogen, can markedly inhibit T-cell function in vitro. We now report that the virus potently induces interleukin-10 (IL-10) production by peripheral blood mononuclear cells. The IL-10 produced contributes to viral inhibition of T-cell proliferation and protects T cells from PIV3-mediated apoptosis. These findings suggest that IL-10 is likely to play an important immunoregulatory role in PIV3 infections.

Adult↗
PubMed2002

Evaluation of the replication and immunogenicity of recombinant human parainfluenza virus type 3 vectors expressing up to three foreign glycoproteins.

The level of replication and immunogenicity of recombinant parainfluenza virus type 3 (rHPIV3) bearing one, two, or three gene insertions expressing foreign protective antigens was examined. cDNA-derived recombinant HPIV3s bearing genes encoding the open reading frames (ORFs) of the hemagglutinin-neuraminidase (HN) of HPIV1, the HN of HPIV2, or the hemagglutinin (HA) of measles virus replicated efficiently in vitro, including the largest recombinant, which had three gene unit insertions and which was almost 23 kb in length, 50% longer than unmodified HPIV3. Several viruses were recovered from cDNAs whose genome length was not a multiple of six nucleotides and these contained nucleotide insertions that corrected the length to be a multiple of 6, confirming that the "rule of six" applies to HPIV3. Using a hemagglutination inhibition assay, we determined that the HPIV1 HN expressed by recombinant HPIV3 was incorporated into HPIV3 virions, whereas using this assay incorporation of the HPIV2 HN could not be detected. HPIV3 virions bearing HPIV1 HN were not neutralized by HPIV1 antiserum but were readily neutralized by antibodies to the HPIV3 HN or fusion protein (F). Viruses with inserts were restricted for replication in the respiratory tract of hamsters, and the level of restriction was a function of the total number of genes inserted, the nature of the insert, and the position of the inserted gene in the gene order. A single insert of HPIV2 HN or measles virus HA reduced the in vivo replication of rHPIV3 up to 25-fold, whereas the HPIV1 HN insert decreased replication almost 1000-fold. This indicates that the HPIV1 HN insert has an attenuating effect in addition to that of the extra gene insert itself, presumably because it is incorporated into the virus particle. Viruses containing two inserts were generally more attenuated than those with a single insert, and viruses with three inserts were over-attenuated for replication in hamsters. Inserts between the N and P genes were slightly more attenuating than those between the P and the M genes. A recombinant HPIV3 bearing both the HPIV1 and the HPIV2 HN genes (r1HN 2HN) was attenuated, immunogenic, and protected immunized hamsters from challenge with HPIV1, HPIV2, and HPIV3. Thus, it is possible to use a single HPIV vector expressing two foreign gene inserts to protect infants and young children from the severe lower respiratory tract disease caused by the three major human PIV pathogens.

Animals↗
PubMed1996

Semi-permissive replication and functional aspects of the immune response in a cotton rat model of human parainfluenza virus type 3 infection.

A cotton rat (Sigmodon fulviventer) model of human parainfluenza virus type 3 (HPIV-3) infection was used to study patterns of HPIV-3 replication in naive and immune hosts. Growth curves revealed that nasal and pulmonary tissues of naive animals were semi-permissive for virus replication, with amounts of progeny virus proportional to inoculating doses. In naive animals there was a total eclipse in nasal tissues beginning 4 h after inoculation. By contrast, there was only partial eclipse of virus in pulmonary tissues, most pronounced at 1 h after inoculation. Immune animals demonstrated a delayed eclipse in pulmonary tissues upon rechallenge. Infection with very low doses of HPIV-3 induced complete protection against high-dose challenge in the absence of systemic neutralizing antibody, suggesting a significant role for other systemic or local immune effectors.

Animals↗
PubMed1999

The use of a quantitative fusion assay to evaluate HN-receptor interaction for human parainfluenza virus type 3.

Sialic acid is the receptor determinant for the human parainfluenza virus type 3 (HPF3) hemagglutinin-neuraminidase (HN) glycoprotein, the molecule responsible for binding of the virus to cell surfaces. In order for the fusion protein (F) of HPF3 to promote membrane fusion, HN must interact with its receptor. In addition to its role in receptor binding and fusion promotion, the HPF3 HN molecule contains receptor-destroying (sialidase) activity. The putative active sites are in the extracellular domain of this type II integral membrane protein. However, HN is not available in crystalline form; the exact locations of these sites, and the structural requirements for binding to the cellular receptor, which has not yet been isolated, are unknown. Nor have small molecular synthetic inhibitors of attachment or fusion that would provide insight into these processes been identified. The strategy in the present study was to develop an assay system that would provide a measure of a specific step in the viral cycle-functional interaction between viral glycoproteins and the cell during attachment and fusion-and serve to screen a variety of substances for inhibitory potential. The assay is based on our previous finding that CV-1 cells persistently infected (p.i.) with HPF3 do not fuse with one another but that the addition of uninfected CV-1 cells, supplying the critical sialic acid containing receptor molecules that bind HN, results in rapid fusion. In the present assay two HeLa cell types were used: we persistently infected HeLa-LTR-betagal cells, assessed their fusion with uninfected HeLa-tat cells, and then quantitated the beta-galactosidase (betagal) produced as a result of this fusion. The analog alpha-2-S-methyl-5-N-thioacetylneuraminic acid (alpha-Neu5thioAc2SMe) interfered with fusion, decreasing betagal production by 84% at 50 mM and by 24% at 25 mM. In beginning to extend our studies to different types of molecules, we tested an unsaturated derivative of sialic acid, 2,3-dehydro-2-deoxy-n-acetyl neuraminic acid (DANA), which is known to inhibit influenza neuraminidase by virtue of being a transition-state analog. We found that 10 mM DANA inhibited neuraminidase activity in HPF3 viral preparations. More significantly, this compound was active in our assay of HN-receptor interaction; 10 mM DANA completely blocked fusion and betagal production, and hemadsorption inhibition by DANA suggested that DANA blocks attachment. In plaque reduction assays performed with the compounds, the active analog alpha-Neu5thioAc2SMe reduced plaque formation by 50% at a 50 mM concentration; DANA caused a 90% inhibition in the plaque reduction assay at a concentration of 25 mM. Our results indicate that specific sialic acid analogs that mimic the cellular receptor determinant of HPF3 can block virus cell interaction and that an unsaturated n-acetyl-neuraminic acid derivative with affinity to the HN site responsible for neuraminidase activity also interferes with HN-receptor binding. Strategies suggested by these findings are now being pursued to obtain information regarding the relative locations of the active sites of HN and to further elucidate the relationship between the receptor-binding and receptor-destroying activities of HN during the viral life cycle. The quantitative assay that we describe is of immediate applicability to large-scale screening for potential inhibitors of HPF3 infection in vivo.

Animals↗
PubMed1993

Role of cellular actin in human parainfluenza virus type 3 genome transcription.

The transcribing ribonucleoprotein (RNP) complex of human parainfluenza virus type 3 (HPIV-3) requires cellular actin for transcription of viral genome in vitro (De, B. P., Lesoon, A., and Banerjee, A. K. (1991) J. Virol. 65, 3268-3275). In this communication, we have studied the interactions between different molecular forms of actin and the RNP of HPIV-3 to understand the role of actin in mRNA synthesis. We demonstrate that both polymeric and monomeric forms of actin (obtained by DNase I treatment) bind strongly to the RNP at 100 mM KCl concentration (polymerizing buffer). The binding was virtually abolished at zero KCl concentration (depolymerizing buffer). Isolation of the RNP-actin complex and subsequent use in a transcription reaction showed that the bound actin alone was sufficient for mRNA synthesis in vitro. Interestingly, the DNase I-arrested monomeric form of actin failed to activate mRNA synthesis, indicating a requirement of polymerization of the bound actin during HPIV-3 transcription. Electron microscopic analyses revealed that a drastic structural modification of the RNP occurred because of the polymerization of actin from a loosely coiled and irregular structure to a condensed and flexible structure. Activation of transcription was observed also with poly-L-glutamic acid, a highly acidic polypeptide. However, unlike cellular actin, poly-L glutamic acid was able to activate only 10% of the input RNP. These results suggest that cellular actin activates HPIV-3 transcription by polymerizing specifically on the RNP complex. This event results in an alteration of the RNP structure that enhances its suitability for efficient transcription. The acidic domain of actin may play an important role in this process.

Actins↗
PubMed2000

Replacement of the ectodomains of the hemagglutinin-neuraminidase and fusion glycoproteins of recombinant parainfluenza virus type 3 (PIV3) with their counterparts from PIV2 yields attenuated PIV2 vaccine candidates.

We sought to develop a live attenuated parainfluenza virus type 2 (PIV2) vaccine strain for use in infants and young children, using reverse genetic techniques that previously were used to rapidly produce a live attenuated PIV1 vaccine candidate. The PIV1 vaccine candidate, designated rPIV3-1cp45, was generated by substituting the full-length HN and F proteins of PIV1 for those of PIV3 in the attenuated cp45 PIV3 vaccine candidate (T. Tao et al., J. Virol. 72:2955-2961, 1998; M. H. Skiadopoulos et al., Vaccine 18:503-510, 1999). However, using the same strategy, we failed to recover recombinant chimeric PIV3-PIV2 isolate carrying the full-length PIV2 glycoproteins in a wild-type PIV3 backbone. Viable PIV3-PIV2 chimeras were recovered when chimeric HN and F open reading frames (ORFs) rather than complete PIV2 F and HN ORFs were used to construct the full-length cDNA. The recovered viruses, designated rPIV3-2CT, in which the PIV2 ectodomain and transmembrane domain were fused to the PIV3 cytoplasmic domain, and rPIV3-2TM, in which the PIV2 ectodomain was fused to the PIV3 transmembrane and cytoplasmic tail domain, possessed similar in vitro and in vivo phenotypes. Thus, it appeared that only the cytoplasmic tail of the HN or F glycoprotein of PIV3 was required for successful recovery of PIV3-PIV2 chimeras. Although rPIV3-2CT and rPIV3-2TM replicated efficiently in vitro, they were moderately to highly attenuated for replication in the respiratory tracts of hamsters, African green monkeys (AGMs), and chimpanzees. This unexpected finding indicated that chimerization of the HN and F proteins of PIV2 and PIV3 itself specified an attenuation phenotype in vivo. Despite this attenuation, these viruses were highly immunogenic and protective against challenge with wild-type PIV2 in hamsters and AGMs, and they represent promising candidates for clinical evaluation as a vaccine against PIV2. These chimeric viruses were further attenuated by the addition of 12 mutations of PIV3cp45 which lie outside of the HN and F genes. The attenuating effects of these mutations were additive with that of the chimerization, and thus inclusion of all or some of the cp45 mutations provides a means to further attenuate the PIV3-PIV2 chimeric vaccine candidates if necessary.

Amino Acid Sequence↗
PubMed2001

Inhibition of human parainfluenza virus type 1 sialidase by analogs of 2-deoxy-2,3-didehydro-N-acetylneuraminic acid.

Eleven novel analogs of 2-deoxy-2,3-didehydro-N-acetylneuraminic acid (Neu5Ac2en) modified at the C-4 and C-9 positions were designed and tested for their ability to inhibit sialidase of human parainfluenza virus type 1 (hPIV-1). The analogs modified by the cyanomethyl, amidinomethyl, and thiocarbamoylmethyl groups at the C-4 position exhibited potent inhibition against hPIV-1 sialidase compared with Neu5Ac2en. The most effective compound was thiocarbamoylmethyl analog (4-O-thiocarbamoylmethyl-Neu5Ac2en). The activity of 4-O-thiocarbamoylmethyl-Neu5Ac2en causing 50% enzyme inhibition at a concentration of approximately 1.0x10(-5) M was 30-fold larger than Neu5Ac2en. While, the analogs of Neu5Ac2en modified by the azido and N-acetyl groups at the C-9 showed a decrease in inhibition of sialidase compared with the 9-hydroxy analogs. In addition, 4-O-thiocarbamoylmethyl-Neu5Ac2en strongly inhibited hPIV-1 infections of Lewis lung carcinoma-monkey kidney cells in comparison with Neu5Ac2en. The present findings would provide useful information for the development of anti-human parainfluenza virus compounds.

Animals↗
PubMed1986

Protection of weanling hamsters from experimental infection with wild-type parainfluenza virus type 3 (para 3) by cold-adapted mutants of para 3.

Parainfluenza virus type 3 (para 3) was adapted to replicate at 20 degrees C, a nonpermissive temperature for wild-type (wt) para 3. Serial passage at 20 degrees C resulted in the generation of cold-adapted (ca) and temperature-sensitive (ts) mutants. These mutant viruses have been characterized both in vitro and in vivo [Belshe and Hissom (1982): Journal of Medical Virology 10:235-242; Crookshanks and Belshe (1984): Journal of Medical Virology 13:243-249]. We now report the evaluation of three mutants (clone 1150, passaged 12 times in the cold [cp12], clone 1146, passaged 18 times in the cold [cp18], and clone 1328, passaged 45 times in the cold [cp45]) for their ability to protect hamsters from infection by wild-type para 3. Ether-anesthetized male syrian hamsters were intranasally vaccinated with either wt para 3 (clone 127) or one of the ca para 3 mutants and on day 28 post-vaccination; each animal was intranasally challenged with 10(5.0) pfu of wt para 3. On days 1, 2, 3, and 4 post-challenge, 4 to 13 hamsters from each group were sacrificed, and the quantity of para 3 in the nasal turbinates and lungs was determined. Wt virus induced protection from challenge. cp12, cp18, and cp45 reduced the peak titer of wt replication in the lungs by greater than 100-fold, tenfold, and tenfold, respectively. The duration of virus replication was shortened also by intranasal vaccination with the mutants. These data give evidence of an inverse relationship between the degree of protection induced by vaccination with cold-adapted mutants and the number of passages of the virus in the cold.

Administration, Intranasal↗
PubMed2001

A chimeric human-bovine parainfluenza virus type 3 expressing measles virus hemagglutinin is attenuated for replication but is still immunogenic in rhesus monkeys.

The chimeric recombinant virus rHPIV3-N(B), a version of human parainfluenza virus type 3 (HPIV3) that is attenuated due to the presence of the bovine PIV3 nucleocapsid (N) protein open reading frame (ORF) in place of the HPIV3 ORF, was modified to encode the measles virus hemagglutinin (HA) inserted as an additional, supernumerary gene between the HPIV3 P and M genes. This recombinant, designated rHPIV3-N(B)HA, replicated like its attenuated rHPIV3-N(B) parent virus in vitro and in the upper and lower respiratory tracts of rhesus monkeys, indicating that the insertion of the measles virus HA did not further attenuate rHPIV3-N(B) in vitro or in vivo. Monkeys immunized with rHPIV3-N(B)HA developed a vigorous immune response to both measles virus and HPIV3, with serum antibody titers to both measles virus (neutralizing antibody) and HPIV3 (hemagglutination inhibiting antibody) of over 1:500. An attenuated HPIV3 expressing a major protective antigen of measles virus provides a method for immunization against measles by the intranasal route, a route that has been shown with HPIV3 and respiratory syncytial virus vaccines to be relatively refractory to the neutralizing and immunosuppressive effects of maternally derived virus-specific serum antibodies. It should now be possible to induce a protective immune response against measles virus in 6-month-old infants, an age group that in developing areas of the world is not responsive to the current measles virus vaccine.

Animals↗
PubMed2004

Safety and immunogenicity of intranasal murine parainfluenza virus type 1 (Sendai virus) in healthy human adults.

Human parainfluenza virus-type 1 (hPIV-1) is the most common cause of pediatric laryngotracheobronchitis (croup) and results in close to 30,000 US hospitalizations each year. No effective vaccine is available. We examined murine PIV-1 (Sendai virus, SeV) as a live, xenotropic vaccine for the closely related human PIV-1 in a phase I, dose escalation study in healthy adults. Intranasal Sendai virus was uniformly well-tolerated and showed evidence of immunogenicity in three of nine vaccinees despite pre-existing, cross-reactive immunity presumably induced by previous exposure to human PIV-1. Results encourage future trials to evaluate the efficacy of Sendai virus in preventing human PIV-1 infection in infants and children.

Administration, Intranasal↗
PubMed2000

Detection and identification of human parainfluenza viruses 1, 2, 3, and 4 in clinical samples of pediatric patients by multiplex reverse transcription-PCR.

We describe a multiplex reverse transcription-PCR (m-RT-PCR) assay that is able to detect and differentiate all known human parainfluenza viruses (HPIVs). Serial dilution experiments with reference strains that compared cell culture isolation and m-RT-PCR showed sensitivities ranging from 0.0004 50% tissue culture infective dose (TCID(50)) for HPIV type 4B (HPIV-4B) to 32 TCID(50)s for HPIV-3. As few as 10 plasmids containing HPIV PCR products could be detected in all cases. When 201 nasopharyngeal aspirate specimens from pediatric patients hospitalized for lower respiratory illness were tested, m-RT-PCR assay detected 64 HPIVs (24 HPIV-3, 23 HPIV-1, 10 HPIV-4, and 7 HPIV-2), while only 42 of them (21 HPIV-1, 14 HPIV-3, 6 HPIV-2, and 1 HPIV-4 isolates) grew in cell culture. Our m-RT-PCR assay was more sensitive than either cell culture isolation or indirect immunofluorescence with monoclonal antibodies for the detection of HPIV infections. Also, HPIV-4 was more frequently detected than HPIV-2 in this study, suggesting that it may have been underestimated as a lower respiratory tract pathogen because of the insensitivity of cell culture.

Animals↗