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Article ; Online: Hepatitis a Vaccine Promotion Using Facebook Ads to Reach At-Risk Groups.

Schwartz, Pamela / Sedillo, Jennifer L / Sapp, Jessica L C

American journal of health promotion : AJHP

2021 Volume 36, Issue 2, Page(s) 296–300

Abstract: Purpose: To evaluate using Facebook ads to promote hepatitis A vaccination to at-risk groups.: Design: This descriptive research study used Facebook ads and posts to deliver a social media health campaign.: Setting: The social networking site ... ...

Abstract	Purpose: To evaluate using Facebook ads to promote hepatitis A vaccination to at-risk groups. Design: This descriptive research study used Facebook ads and posts to deliver a social media health campaign. Setting: The social networking site Facebook was used to target audiences in the United States. Subjects: Adults in the United States with Facebook accounts were the general audience with at-risk audiences having interests or profile attributes in either LGBTQ or food service groups. Measures: Facebook Ads Manager was used to determine impressions, engagement rates, link clicks, and cost per result of the ads. These metrics were measured to examine the use of Facebook ads and targeting audiences. Analysis: Quantitative data were analyzed using descriptive statistics, and the Pearson correlation coefficient analysis was used to determine if the amount spent on each ad had any correlation with reach, results, cost per result, or impressions. Results: The campaign resulted in a reach of 53 422 users, 70 542 impressions, 457 unique link clicks (483 link clicks), an average cost per results of $0.92 USD, and the total amount spent of $445.68 USD. The amount spent was positively correlated with reach (r = .969), results (r = .994), cost per result (r = .841), and impressions (r =.957). Conclusion: The social media health campaign was effective in reaching an audience about hepatitis A vaccination. Using interest groups was not more cost-effective than a using a general audience for link clicks.
MeSH term(s)	Adult ; Advertising/methods ; Health Promotion/methods ; Hepatitis A Vaccines ; Humans ; Social Media ; Social Networking ; United States
Chemical Substances	Hepatitis A Vaccines
Language	English
Publishing date	2021-11-23
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	645160-3
ISSN	2168-6602 ; 0890-1171
ISSN (online)	2168-6602
ISSN	0890-1171
DOI	10.1177/08901171211044594
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Article: The development of point-of-use water filters as sampling devices in bioforensics: extent of microbial sorption and elution

Sedillo, Jennifer L / Quintana, Ayshea / Souza, Kathryn / Oshima, Kevin H / Smith, Geoffrey B

Journal of environmental monitoring. 2008 June 1, v. 10, no. 6

2008

Abstract: The foundational idea for this project is that household faucet-mounted water filters may be used as bioforensic sampling devices to detect the extent of a potential bioagent release in domestic water supplies. An optimized eluent solution was determined ...

Abstract	The foundational idea for this project is that household faucet-mounted water filters may be used as bioforensic sampling devices to detect the extent of a potential bioagent release in domestic water supplies. An optimized eluent solution was determined experimentally by quantifying recoveries of microorganisms from point-of-use (POU) drinking water filters. The optimized extraction protocol was then used in mock bioagent release experiments to determine the feasibility of POU filters as bioforensic sampling devices. Bacillus atrophaeus spores, Escherichia coli and PP7 virus were exposed to filters and the number of attached organisms was determined by enumerating the unattached organisms on selective agar media. Subsequently, the filters were eluted and the percent of extracted organisms was determined based on the number of attached organisms. Two popular brands of carbon block filters retained 92%–99% of representative virus, spore and vegetative bacteria. In back-flush elutions of single filters, the most efficient eluent was identified as a combination of 1% peptone and 1% Tween-80, and extraction recovered 25.4% (±17.5%) of attached E. coli, 20.4% (±3.6%) of B. atrophaeus spores, and 9.4% (±5.2%) of PP7 virions (± standard deviations). In bioagent release studies in which filters were challenged with 100 agents mL−1, greater than 99% of the spores were retained by the filters, and the percent of attached spores that were recovered ranged from 10.4% at day 0 to 4.3% five days after the release event (averaged from five separate experiments). In contrast, E. coli, Salmonella typhimurium and PP7 virus were rapidly inactivated in the chlorinated tap water, indicating their improbable survival in chlorinated water supplies. It is therefore concluded that household water filters can be used as microbial sampling devices for bioforensic applications in the event of a bioagent release in domestic drinking water supplies.
Keywords	Bacillus atrophaeus ; Escherichia coli ; Salmonella Typhimurium ; bacteria ; carbon ; peptones ; polysorbates ; selective media ; sorption ; spores ; standard deviation ; tap water ; virion ; viruses ; water filters ; water supply
Language	English
Dates of publication	2008-0601
Size	p. 718-723.
Publishing place	The Royal Society of Chemistry
Document type	Article
ZDB-ID	1453583-x
ISSN	1464-0333 ; 1464-0325
ISSN (online)	1464-0333
ISSN	1464-0325
DOI	10.1039/b718064k
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Identification of a bacteriocin and its cognate immunity factor expressed by Moraxella catarrhalis

Liu Wei / Hoopman Todd C / Sedillo Jennifer L / Attia Ahmed S / Liu Lixia / Brautigam Chad A / Hansen Eric J

BMC Microbiology, Vol 9, Iss 1, p

2009 Volume 207

Abstract: Abstract Background Bacteriocins are antimicrobial proteins and peptides ribosomally synthesized by some bacteria which can effect both intraspecies and interspecies killing. Results Moraxella catarrhalis strain E22 containing plasmid pLQ510 was shown to ...

Abstract	Abstract Background Bacteriocins are antimicrobial proteins and peptides ribosomally synthesized by some bacteria which can effect both intraspecies and interspecies killing. Results Moraxella catarrhalis strain E22 containing plasmid pLQ510 was shown to inhibit the growth of M. catarrhalis strain O35E. Two genes ( mcbA and mcbB ) in pLQ510 encoded proteins predicted to be involved in the secretion of a bacteriocin. Immediately downstream from these two genes, a very short ORF ( mcbC ) encoded a protein which had some homology to double-glycine bacteriocins produced by other bacteria. A second very short ORF ( mcbI ) immediately downstream from mcbC encoded a protein which had no significant similarity to other proteins in the databases. Cloning and expression of the mcbI gene in M. catarrhalis O35E indicated that this gene encoded the cognate immunity factor. Reverse transcriptase-PCR was used to show that the mcbA , mcbB , mcbC , and mcbI ORFs were transcriptionally linked. This four-gene cluster was subsequently shown to be present in the chromosome of several M. catarrhalis strains including O12E. Inactivation of the mcbA , mcbB , or mcbC ORFs in M. catarrhalis O12E eliminated the ability of this strain to inhibit the growth of M. catarrhalis O35E. In co-culture experiments involving a M. catarrhalis strain containing the mcbABCI locus and one which lacked this locus, the former strain became the predominant member of the culture after overnight growth in broth. Conclusion This is the first description of a bacteriocin and its cognate immunity factor produced by M. catarrhalis . The killing activity of the McbC protein raises the possibility that it might serve to lyse other M. catarrhalis strains that lack the mcbABCI locus, thereby making their DNA available for lateral gene transfer.
Keywords	Microbiology ; QR1-502 ; Science ; Q ; DOAJ:Microbiology ; DOAJ:Biology ; DOAJ:Biology and Life Sciences
Subject code	572
Language	English
Publishing date	2009-09-01T00:00:00Z
Publisher	BioMed Central
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: The development of point-of-use water filters as sampling devices in bioforensics: extent of microbial sorption and elution.

Sedillo, Jennifer L / Quintana, Ayshea / Souza, Kathryn / Oshima, Kevin H / Smith, Geoffrey B

Journal of environmental monitoring : JEM

2008 Volume 10, Issue 6, Page(s) 718–723

Abstract	The foundational idea for this project is that household faucet-mounted water filters may be used as bioforensic sampling devices to detect the extent of a potential bioagent release in domestic water supplies. An optimized eluent solution was determined experimentally by quantifying recoveries of microorganisms from point-of-use (POU) drinking water filters. The optimized extraction protocol was then used in mock bioagent release experiments to determine the feasibility of POU filters as bioforensic sampling devices. Bacillus atrophaeus spores, Escherichia coli and PP7 virus were exposed to filters and the number of attached organisms was determined by enumerating the unattached organisms on selective agar media. Subsequently, the filters were eluted and the percent of extracted organisms was determined based on the number of attached organisms. Two popular brands of carbon block filters retained 92%-99% of representative virus, spore and vegetative bacteria. In back-flush elutions of single filters, the most efficient eluent was identified as a combination of 1% peptone and 1% Tween-80, and extraction recovered 25.4% (+/-17.5%) of attached E. coli, 20.4% (+/-3.6%) of B. atrophaeus spores, and 9.4% (+/-5.2%) of PP7 virions (+/- standard deviations). In bioagent release studies in which filters were challenged with 100 agents mL(-1), greater than 99% of the spores were retained by the filters, and the percent of attached spores that were recovered ranged from 10.4% at day 0 to 4.3% five days after the release event (averaged from five separate experiments). In contrast, E. coli, Salmonella typhimurium and PP7 virus were rapidly inactivated in the chlorinated tap water, indicating their improbable survival in chlorinated water supplies. It is therefore concluded that household water filters can be used as microbial sampling devices for bioforensic applications in the event of a bioagent release in domestic drinking water supplies.
MeSH term(s)	Adsorption ; Animals ; Bacillus/isolation & purification ; Bacteria/isolation & purification ; Bacteriophages/isolation & purification ; Colony Count, Microbial ; Escherichia coli/isolation & purification ; Filtration/instrumentation ; Filtration/methods ; Humans ; Risk Assessment ; Salmonella typhimurium/isolation & purification ; Water Microbiology ; Water Purification/instrumentation ; Water Purification/methods ; Water Supply
Language	English
Publishing date	2008-06
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	1453583-x
ISSN	1464-0333 ; 1464-0325
ISSN (online)	1464-0333
ISSN	1464-0325
DOI	10.1039/b718064k
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Moraxella catarrhalis Expresses an Unusual Hfq Protein

Attia, Ahmed S / Sedillo, Jennifer L / Wang, Wei / Liu, Wei / Brautigam, Chad A / Winkler, Wade / Hansen, Eric J

Infection and immunity. 2008 June, v. 76, no. 6

2008

Abstract: The Hfq protein is recognized as a global regulatory molecule that facilitates certain RNA-RNA interactions in bacteria. BLAST analysis identified a 630-nucleotide open reading frame in the genome of Moraxella catarrhalis ATCC 43617 that was highly ... ...

Abstract	The Hfq protein is recognized as a global regulatory molecule that facilitates certain RNA-RNA interactions in bacteria. BLAST analysis identified a 630-nucleotide open reading frame in the genome of Moraxella catarrhalis ATCC 43617 that was highly conserved among M. catarrhalis strains and which encoded a predicted protein with significant homology to the Hfq protein of Escherichia coli. This protein, containing 210 amino acids, was more than twice as large as the Hfq proteins previously described for other bacteria. The C-terminal half of the M. catarrhalis Hfq protein was very hydrophilic and contained two different types of amino acid repeats. A mutation in the M. catarrhalis hfq gene affected both the growth rate of this organism and its sensitivity to at least two different types of stress in vitro. Provision of the wild-type M. catarrhalis hfq gene in trans eliminated these phenotypic differences in the hfq mutant. This M. catarrhalis hfq mutant exhibited altered expression of some cell envelope proteins relative to the wild-type parent strain and also had a growth advantage in a continuous flow biofilm system. The presence of the wild-type M. catarrhalis hfq gene in trans in an E. coli hfq mutant fully reversed the modest growth deficiency of this E. coli mutant and partially reversed the stress sensitivity of this E. coli mutant to methyl viologen. The use of an electrophoretic mobility shift assay showed that this M. catarrhalis Hfq protein could bind RNA derived from a gene whose expression was altered in the M. catarrhalis hfq mutant.
Keywords	Escherichia coli ; Moraxella catarrhalis ; RNA ; amino acids ; bacteria ; bacterial proteins ; biofilm ; electrophoresis ; genes ; mutants ; mutation ; open reading frames ; paraquat
Language	English
Size	p. 2520-2530.
Publishing place	American Society for Microbiology
Document type	Article
ZDB-ID	218698-6
ISSN	1098-5522 ; 0019-9567
ISSN (online)	1098-5522
ISSN	0019-9567
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Identification of a bacteriocin and its cognate immunity factor expressed by Moraxella catarrhalis.

Attia, Ahmed S / Sedillo, Jennifer L / Hoopman, Todd C / Liu, Wei / Liu, Lixia / Brautigam, Chad A / Hansen, Eric J

BMC microbiology

2009 Volume 9, Page(s) 207

Abstract: Background: Bacteriocins are antimicrobial proteins and peptides ribosomally synthesized by some bacteria which can effect both intraspecies and interspecies killing.: Results: Moraxella catarrhalis strain E22 containing plasmid pLQ510 was shown to ... ...

Abstract	Background: Bacteriocins are antimicrobial proteins and peptides ribosomally synthesized by some bacteria which can effect both intraspecies and interspecies killing. Results: Moraxella catarrhalis strain E22 containing plasmid pLQ510 was shown to inhibit the growth of M. catarrhalis strain O35E. Two genes (mcbA and mcbB) in pLQ510 encoded proteins predicted to be involved in the secretion of a bacteriocin. Immediately downstream from these two genes, a very short ORF (mcbC) encoded a protein which had some homology to double-glycine bacteriocins produced by other bacteria. A second very short ORF (mcbI) immediately downstream from mcbC encoded a protein which had no significant similarity to other proteins in the databases. Cloning and expression of the mcbI gene in M. catarrhalis O35E indicated that this gene encoded the cognate immunity factor. Reverse transcriptase-PCR was used to show that the mcbA, mcbB, mcbC, and mcbI ORFs were transcriptionally linked. This four-gene cluster was subsequently shown to be present in the chromosome of several M. catarrhalis strains including O12E. Inactivation of the mcbA, mcbB, or mcbC ORFs in M. catarrhalis O12E eliminated the ability of this strain to inhibit the growth of M. catarrhalis O35E. In co-culture experiments involving a M. catarrhalis strain containing the mcbABCI locus and one which lacked this locus, the former strain became the predominant member of the culture after overnight growth in broth. Conclusion: This is the first description of a bacteriocin and its cognate immunity factor produced by M. catarrhalis. The killing activity of the McbC protein raises the possibility that it might serve to lyse other M. catarrhalis strains that lack the mcbABCI locus, thereby making their DNA available for lateral gene transfer.
MeSH term(s)	Amino Acid Sequence ; Antibiosis ; Bacteriocins/genetics ; Bacteriocins/immunology ; Cloning, Molecular ; DNA, Bacterial/genetics ; Gene Expression Regulation, Bacterial ; Genes, Bacterial ; Molecular Sequence Data ; Moraxella catarrhalis/genetics ; Moraxella catarrhalis/immunology ; Multigene Family ; Open Reading Frames ; Plasmids ; Sequence Deletion
Chemical Substances	Bacteriocins ; DNA, Bacterial
Language	English
Publishing date	2009-09-25
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ISSN	1471-2180
ISSN (online)	1471-2180
DOI	10.1186/1471-2180-9-207
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Moraxella catarrhalis expresses an unusual Hfq protein.

Attia, Ahmed S / Sedillo, Jennifer L / Wang, Wei / Liu, Wei / Brautigam, Chad A / Winkler, Wade / Hansen, Eric J

Infection and immunity

2008 Volume 76, Issue 6, Page(s) 2520–2530

Abstract	The Hfq protein is recognized as a global regulatory molecule that facilitates certain RNA-RNA interactions in bacteria. BLAST analysis identified a 630-nucleotide open reading frame in the genome of Moraxella catarrhalis ATCC 43617 that was highly conserved among M. catarrhalis strains and which encoded a predicted protein with significant homology to the Hfq protein of Escherichia coli. This protein, containing 210 amino acids, was more than twice as large as the Hfq proteins previously described for other bacteria. The C-terminal half of the M. catarrhalis Hfq protein was very hydrophilic and contained two different types of amino acid repeats. A mutation in the M. catarrhalis hfq gene affected both the growth rate of this organism and its sensitivity to at least two different types of stress in vitro. Provision of the wild-type M. catarrhalis hfq gene in trans eliminated these phenotypic differences in the hfq mutant. This M. catarrhalis hfq mutant exhibited altered expression of some cell envelope proteins relative to the wild-type parent strain and also had a growth advantage in a continuous flow biofilm system. The presence of the wild-type M. catarrhalis hfq gene in trans in an E. coli hfq mutant fully reversed the modest growth deficiency of this E. coli mutant and partially reversed the stress sensitivity of this E. coli mutant to methyl viologen. The use of an electrophoretic mobility shift assay showed that this M. catarrhalis Hfq protein could bind RNA derived from a gene whose expression was altered in the M. catarrhalis hfq mutant.
MeSH term(s)	Amino Acid Sequence ; Biofilms ; Escherichia coli ; Gene Expression Regulation, Bacterial/physiology ; Genetic Complementation Test ; Host Factor 1 Protein/chemistry ; Host Factor 1 Protein/genetics ; Host Factor 1 Protein/metabolism ; Molecular Sequence Data ; Moraxella catarrhalis/genetics ; Moraxella catarrhalis/growth & development ; Moraxella catarrhalis/metabolism ; Mutation ; Protein Binding ; RNA/metabolism
Chemical Substances	Host Factor 1 Protein ; RNA (63231-63-0)
Language	English
Publishing date	2008-03-24
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	218698-6
ISSN	1098-5522 ; 0019-9567
ISSN (online)	1098-5522
ISSN	0019-9567
DOI	10.1128/IAI.01652-07
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Modular arrangement of allelic variants explains the divergence in Moraxella catarrhalis UspA protein function.

Brooks, Michael J / Sedillo, Jennifer L / Wagner, Nikki / Laurence, Cassie A / Wang, Wei / Attia, Ahmed S / Hansen, Eric J / Gray-Owen, Scott D

Infection and immunity

2008 Volume 76, Issue 11, Page(s) 5330–5340

Abstract: Ubiquitous surface protein A molecules (UspAs) of Moraxella catarrhalis are large, nonfimbrial, autotransporter proteins that can be visualized as a "fuzzy" layer on the bacterial surface by transmission electron microscopy. Previous studies attributed a ...

Abstract	Ubiquitous surface protein A molecules (UspAs) of Moraxella catarrhalis are large, nonfimbrial, autotransporter proteins that can be visualized as a "fuzzy" layer on the bacterial surface by transmission electron microscopy. Previous studies attributed a wide array of functions and binding activities to the closely related UspA1, UspA2, and/or UspA2H protein, yet the molecular and phylogenetic relationships among these activities remain largely unexplored. To address this issue, we determined the nucleotide sequence of the uspA1 genes from a variety of independent M. catarrhalis isolates and compared the deduced amino acid sequences to those of the previously characterized UspA1, UspA2, and UspA2H proteins. Rather than being conserved proteins, we observed a striking divergence of individual UspA1, UspA2, and UspA2H proteins resulting from the modular assortment of unrelated "cassettes" of peptide sequence. The exchange of certain variant cassettes correlates with strain-specific differences in UspA protein function and confers differing phenotypes upon these mucosal surface pathogens.
MeSH term(s)	Amino Acid Motifs/genetics ; Amino Acid Sequence ; Bacterial Outer Membrane Proteins/chemistry ; Bacterial Outer Membrane Proteins/genetics ; Bacterial Outer Membrane Proteins/metabolism ; Base Sequence ; Consensus Sequence/genetics ; DNA, Bacterial/genetics ; Molecular Sequence Data ; Moraxella catarrhalis/chemistry ; Moraxella catarrhalis/genetics ; Moraxella catarrhalis/metabolism ; Phenotype ; Polymerase Chain Reaction ; Protein Structure, Tertiary/genetics ; Sequence Homology, Amino Acid
Chemical Substances	Bacterial Outer Membrane Proteins ; DNA, Bacterial ; UspA protein, Moraxella catarrhalis
Language	English
Publishing date	2008-08-04
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	218698-6
ISSN	1098-5522 ; 0019-9567
ISSN (online)	1098-5522
ISSN	0019-9567
DOI	10.1128/IAI.00573-08
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Moraxella catarrhalis Binding to Host Cellular Receptors Is Mediated by Sequence-Specific Determinants Not Conserved among All UspA1 Protein Variants

Brooks, Michael J / Sedillo, Jennifer L / Wagner, Nikki / Wang, Wei / Attia, Ahmed S / Wong, Henry / Laurence, Cassie A / Hansen, Eric J / Gray-Owen, Scott D

Infection and immunity. 2008 Nov., v. 76, no. 11

2008

Abstract: The Moraxella catarrhalis ubiquitous surface proteins (UspAs) are autotransporter molecules reported to interact with a variety of different host proteins and to affect processes ranging from serum resistance to cellular adhesion. The role of UspA1 as an ...

Abstract	The Moraxella catarrhalis ubiquitous surface proteins (UspAs) are autotransporter molecules reported to interact with a variety of different host proteins and to affect processes ranging from serum resistance to cellular adhesion. The role of UspA1 as an adhesin has been confirmed with a number of different human cell types and is mediated by binding to eukaryotic proteins including carcinoembryonic antigen-related cellular adhesion molecules (CEACAMs), fibronectin, and laminin. A distinct difference in the ability of prototypical M. catarrhalis strains to adhere to CEACAM-expressing cell lines prompted us to perform strain-specific structure-function analyses of UspA1 proteins. In this study, we characterized CEACAM binding by a diverse set of UspA1 proteins and showed that 3 out of 10 UspA1 proteins were incapable of binding CEACAM. This difference resulted from the absence of a distinct CEACAM binding motif in nonadhering strains. Our sequence analysis also revealed a single M. catarrhalis isolate that lacked the fibronectin-binding motif and was defective in adherence to Chang conjunctival epithelial cells. These results clearly demonstrate that UspA1-associated adhesive functions are not universally conserved. Instead, UspA1 proteins must be considered as variants with the potential to confer both different cell tropisms and host cell responses.
Keywords	Moraxella catarrhalis ; blood serum ; cell adhesion ; epithelial cells ; fibronectins ; humans ; laminin ; receptors ; sequence analysis ; surface proteins ; tropisms
Language	English
Size	p. 5322-5329.
Publishing place	American Society for Microbiology
Document type	Article
ZDB-ID	218698-6
ISSN	1098-5522 ; 0019-9567
ISSN (online)	1098-5522
ISSN	0019-9567
Database	NAL-Catalogue (AGRICOLA)

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Article: Modular Arrangement of Allelic Variants Explains the Divergence in Moraxella catarrhalis UspA Protein Function

Brooks, Michael J / Sedillo, Jennifer L / Wagner, Nikki / Laurence, Cassie A / Wang, Wei / Attia, Ahmed S / Hansen, Eric J / Gray-Owen, Scott D

Infection and immunity. 2008 Nov., v. 76, no. 11

2008

Abstract	Ubiquitous surface protein A molecules (UspAs) of Moraxella catarrhalis are large, nonfimbrial, autotransporter proteins that can be visualized as a "fuzzy" layer on the bacterial surface by transmission electron microscopy. Previous studies attributed a wide array of functions and binding activities to the closely related UspA1, UspA2, and/or UspA2H protein, yet the molecular and phylogenetic relationships among these activities remain largely unexplored. To address this issue, we determined the nucleotide sequence of the uspA1 genes from a variety of independent M. catarrhalis isolates and compared the deduced amino acid sequences to those of the previously characterized UspA1, UspA2, and UspA2H proteins. Rather than being conserved proteins, we observed a striking divergence of individual UspA1, UspA2, and UspA2H proteins resulting from the modular assortment of unrelated "cassettes" of peptide sequence. The exchange of certain variant cassettes correlates with strain-specific differences in UspA protein function and confers differing phenotypes upon these mucosal surface pathogens.
Keywords	Moraxella catarrhalis ; amino acid sequences ; genes ; nucleotide sequences ; pathogens ; phenotype ; phylogeny ; surface proteins ; transmission electron microscopy
Language	English
Size	p. 5330-5340.
Publishing place	American Society for Microbiology
Document type	Article
ZDB-ID	218698-6
ISSN	1098-5522 ; 0019-9567
ISSN (online)	1098-5522
ISSN	0019-9567
Database	NAL-Catalogue (AGRICOLA)

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